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Information on EC 2.1.1.202 - multisite-specific tRNA:(cytosine-C5)-methyltransferase
for references in articles please use BRENDA:EC2.1.1.202
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.202 multisite-specific tRNA:(cytosine-C5)-methyltransferase
IUBMB Comments
The enzyme from Saccharomyces cerevisiae is responsible for complete 5-methylcytosine methylations of yeast tRNA. The incidence of modification depends on the cytosine position in tRNA. At positions 34 and 40, 5-methylcytosine is found only in two yeast tRNAs (tRNALeu(CUA) and tRNAPhe(GAA), respectively), whereas most other elongator yeast tRNAs bear either 5-methylcytosine48 or 5-methylcytosine49, but never both in the same tRNA molecule . The formation of 5-methylcytosine34 and 5-methylcytosine40 is a strictly intron-dependent process, whereas the formation of 5-methylcytosine48 and 5-methylcytosine49 is an intron-independent process [2,3].
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
- 2.1.1.202
- methyltransferases
- mtases
-
methylome
-
williams-beuren
-
anticodon
-
transcriptome-wide
Reaction Schemes
show+
=
+
+
cytosine34 in tRNA precursor
=
+
5-methylcytosine34 in tRNA precursor
+
=
+
+
cytosine40 in tRNA precursor
=
+
5-methylcytosine40 in tRNA precursor
+
cytosine48 in tRNA
=
+
5-methylcytosine48 in tRNA
+
cytosine49 in tRNA
=
+
5-methylcytosine49 in tRNA
Synonyms
trdmt1, nsun6, trm4p, cytosine-5 rna methyltransferase, trm4b, rna:m5c methyltransferase, phnsun6, nop2/sun rna methyltransferase 2, trm4a, m5c rna methyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-methylcytosine RNA methyltransferase
cytosine-5 RNA methyltransferase
EC 2.1.1.29
-
-
formerly, part transferred
-
M5C RNA methyltransferase
NSUN2
PhNSUN6
RNA:m5C methyltransferase
TRDMT1
TRM4
TRM4A
TRM4B
tRNA (cytosine72-C5)-methyltransferase
tRNA:m5C72 MTase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + cytosine34 in tRNA precursor = S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
S-adenosyl-L-methionine + cytosine40 in tRNA precursor = S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA precursor
S-adenosyl-L-methionine + cytosine48 in tRNA = S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
S-adenosyl-L-methionine + cytosine49 in tRNA = S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
S-adenosyl-L-methionine + cytosine34 in tRNA precursor = S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
the formation of 5-methylcytosine34 is a strictly intron-dependent process
S-adenosyl-L-methionine + cytosine34 in tRNA precursor = S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
the enzyme forms a covalent enzyme-substrate intermediate with its target
-
S-adenosyl-L-methionine + cytosine34 in tRNA precursor = S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
-
-
-
-
S-adenosyl-L-methionine + cytosine40 in tRNA precursor = S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA precursor
the formation of 5-methylcytosine34 is a strictly intron-dependent process
S-adenosyl-L-methionine + cytosine40 in tRNA precursor = S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA precursor
the enzyme forms a covalent enzyme-substrate intermediate with its target
-
S-adenosyl-L-methionine + cytosine40 in tRNA precursor = S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA precursor
-
-
-
-
S-adenosyl-L-methionine + cytosine48 in tRNA = S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
the formation of 5-methylcytosine48 is an intron-independent process
S-adenosyl-L-methionine + cytosine48 in tRNA = S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
the enzyme forms a covalent enzyme-substrate intermediate with its target
-
S-adenosyl-L-methionine + cytosine48 in tRNA = S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
-
-
-
-
S-adenosyl-L-methionine + cytosine49 in tRNA = S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
the formation of 5-methylcytosine49 is an intron-independent process
S-adenosyl-L-methionine + cytosine49 in tRNA = S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
the enzyme forms a covalent enzyme-substrate intermediate with its target
-
S-adenosyl-L-methionine + cytosine49 in tRNA = S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
tRNA methylation (yeast)
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (multisite-cytosine-C5)-methyltransferase
The enzyme from Saccharomyces cerevisiae is responsible for complete 5-methylcytosine methylations of yeast tRNA. The incidence of modification depends on the cytosine position in tRNA. At positions 34 and 40, 5-methylcytosine is found only in two yeast tRNAs (tRNALeu(CUA) and tRNAPhe(GAA), respectively), whereas most other elongator yeast tRNAs bear either 5-methylcytosine48 or 5-methylcytosine49, but never both in the same tRNA molecule [1]. The formation of 5-methylcytosine34 and 5-methylcytosine40 is a strictly intron-dependent process, whereas the formation of 5-methylcytosine48 and 5-methylcytosine49 is an intron-independent process [2,3].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + CpG-rich ssRNA (5'-CGCGCGCGCGCG-3')
?
Substrates: m5C methylation directly alters the phosphate backbone in CpG RNA duplex, leading to a C3'-endo to C2'-endo sugar pucker switch of the terminal residues under physiologically-relevant conditions. m5C triggers a B-to-Z DNA, but not A-to-Z, transformation in CpG DNA duplex. The m5C-probe has the sensitivity to detect a single m5C mark change
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine in tRNA precursor
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine in tRNALeu(CAA)
S-adenosyl-L-homocysteine + 5-methylcytosine in tRNALeu(CAA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine15 in vtRNA1.3
S-adenosyl-L-homocysteine + 5-methylcytosine15 in vtRNA1.3
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine27 in vtRNA1.2
S-adenosyl-L-homocysteine + 5-methylcytosine27 in vtRNA1.2
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine27 in vtRNA1.3
S-adenosyl-L-homocysteine + 5-methylcytosine27 in vtRNA1.3
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA
S-adenosyl-L-methionine + cytosine34 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
S-adenosyl-L-methionine + cytosine34 in tRNALeu precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNALeu precursor
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNAPro(CGG)
S-adenosyl-L-methionine + cytosine4( in tRNAPro(AGG)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAPro(AGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine40 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA
S-adenosyl-L-methionine + cytosine40 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA precursor
S-adenosyl-L-methionine + cytosine40 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA precursor
S-adenosyl-L-methionine + cytosine40 in tRNAGly precursor
S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNAGly precursor
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
S-adenosyl-L-methionine + cytosine48 in tRNAAla(AGC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAAla(AGC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAAla(CGC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAAla(CGC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAAla(UGC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAAla(UGC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAAsp precursor
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAAsp precursor
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAAsp(GUC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAAsp(GUC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAAspGTC
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAAspGTC
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAGln(CUG)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAGln(CUG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAGln(UUG)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAGln(UUG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAGlu(CUC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAGlu(CUC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAGlu(UUC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAGlu(UUC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAGly precursor
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAGly precursor
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAGly(CCC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAGly(CCC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAGly(GCC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAGly(GCC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAGly(UCC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAGly(UCC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAGlyGCC
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAGlyGCC
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAHis
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAHis
S-adenosyl-L-methionine + cytosine48 in tRNAHis(GUG)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAHis(GUG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAIle(AAU)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAIle(AAU)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNALeu(AAG)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALeu(AAG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNALeu(CAA)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALeu(CAA)
S-adenosyl-L-methionine + cytosine48 in tRNALeu(CAA) precursor
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALeu(CAA) precursor
Substrates: NSUN2-mediated methylation of C34 of tRNALeu(CAA) has been shown to occur exclusively on intron-containing tRNA precursors
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNALeu(CAG)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALeu(CAG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNALeu(UAA)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALeu(UAA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNALeu(UAG)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALeu(UAG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNALeuCAA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALeuCAA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNALys(CUU)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALys(CUU)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNALys(UUU)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALys(UUU)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAMet(CAU)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAMet(CAU)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAPhe(GAA)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAPhe(GAA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAPro(UGG)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAPro(UGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNASer(AGA)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNASer(AGA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNASer(CGA)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNASer(CGA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNASer(GCU)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNASer(GCU)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNASer(UGA)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNASer(UGA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAThr(AGU)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAThr(AGU)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAThr(CGT)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAThr(CGT)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAThr(UGU)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAThr(UGU)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNATyr(GUA)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNATyr(GUA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAVal(AAC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAVal(AAC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAVal(CAC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAVal(CAC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAVal(UAC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAVal(UAC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
S-adenosyl-L-methionine + cytosine49 in tRNAasp precursor
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAAsp precursor
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAAsp(GUC)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAAsp(GUC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAAspGTC
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAAspGTC
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAGln(CUG)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAGln(CUG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAGln(UUG)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAGln(UUG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAGlu(CUC)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAGlu(CUC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAGlu(UUC)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAGlu(UUC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAGly precursor
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAGly precursor
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAGly(CCC)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAGly(CCC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAGly(GCC)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAGly(GCC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAGly(UCC)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAGly(UCC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAGlyGCC
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAGlyGCC
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNALeuCAA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNALeuCAA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNALys(UUU)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNALys(UUU)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAPhe(GAA)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAPhe(GAA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAPro(AGG)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAPro(AGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAPro(CGG)
S-adenosyl-L-methionine + cytosine49 in tRNAPro(UGG)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAPro(UGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAThr(AGU)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAThr(AGU)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAVal(AAC)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAVal(AAC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAVal(CAC)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAVal(CAC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAVal(UAC)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAVal(UAC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNA
S-adenosyl-L-methionine + cytosine50 in tRNAAspGTC
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAAspGTC
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAGlu(CUC)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAGlu(CUC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAGlu(UUC)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAGlu(UUC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAGly precursor
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAGly precursor
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAGly(CCC)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAGly(CCC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAGly(GCC)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAGly(GCC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAGly(UCC)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAGly(UCC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAGlyGCC
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAGlyGCC
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAHis
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAHis
S-adenosyl-L-methionine + cytosine50 in tRNALeuCAA
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNALeuCAA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAPro(AGG)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAPro(AGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAPro(CGG)
S-adenosyl-L-methionine + cytosine50 in tRNAPro(UGG)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAPro(UGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine59 in vtRNA1.2
S-adenosyl-L-homocysteine + 5-methylcytosine59 in vtRNA1.2
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine59 in vtRNA1.3
S-adenosyl-L-homocysteine + 5-methylcytosine59 in vtRNA1.3
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine69 in vtRNA1.1
S-adenosyl-L-homocysteine + 5-methylcytosine69 in vtRNA1.1
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine72 in tRNACys
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNACys
S-adenosyl-L-methionine + cytosine72 in tRNACys(GCA)
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNACys(GCA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine72 in tRNACys(GCA)-G2A:C71U
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNACys(GCA)-G2A:C71U
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine72 in tRNAThr
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNAThr
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA
Substrates: the enzyme is responsible for complete m5C methylation of yeast tRNA. The frequency of modification depends on the cytosine position in tRNA. At positions 34 and 40, m5C is found only in two yeast tRNAs (tRNALeu (CUA) and tRNAPhe (GAA), respectively), whereas most other elongator yeast tRNAs bear either m5C48 or m5C49, but never both in the same tRNA molecule
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA
-
Substrates: cf. EC 2.1.1.203
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA
-
Substrates: cf. EC 2.1.1.203
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
Substrates: mini-tRNALeu (composed of the anticodon stem-loop extended by the intron) is used to test the formation of m5C34. The formation of m5C34 is strictly intron dependent
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
-
Substrates: the entire intron, or the total precursor tRNA structure, is required for efficient suppressor function of the resultant mature tRNA. The reduced suppressor phenotype is correlated with lack of a 5-methylcytosine modification of the anticodon wobble base
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
Substrates: yeast pre-tRNALeu
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine40 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine40 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA
Substrates: the enzyme is responsible for complete m5C methylation of yeast tRNA. The frequency of modification depends on the cytosine position in tRNA. At positions 34 and 40, m5C is found only in two yeast tRNAs (tRNALeu (CUA) and tRNAPhe (GAA), respectively), whereas most other elongator yeast tRNAs bear either m5C48 or m5C49, but never both in the same tRNA molecule
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine40 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine40 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine40 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA precursor
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine40 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA precursor
Substrates: mini-tRNAPhe (composed of the anticodon stem-loop extended by the intron) is used to test the formation of m5C40. The formation of m5C40 is strictly intron dependent
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine40 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA precursor
-
Substrates: the enzymatic formation of m5C at position 40 in the anticodon stem is strictly dependent on the presence of the intron. Enzymatic formation of m5C40 is independent of the whole architecture of the tRNA molecule and takes place on a minisubstrate composed of the anticodon stem nd loop of yeast tRNAPhe prolonged by its natural 19 nt intron
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine40 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA precursor
-
Substrates: the enzymatic formation of m5C at position 40 in the anticodon stem is strictly dependent on the presence of the intron. Enzymatic formation of m5C40 is independent of the whole architecture of the tRNA molecule and takes place on a minisubstrate composed of the anticodon stem nd loop of yeast tRNAPhe prolonged by its natural 19 nt intron
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
Substrates: the enzyme is responsible for complete m5C methylation of yeast tRNA. The frequency of modification depends on the cytosine position in tRNA. At positions 34 and 40, m5C is found only in two yeast tRNAs (tRNALeu (CUA) and tRNAPhe (GAA), respectively), whereas most other elongator yeast tRNAs bear either m5C48 or m5C49, but never both in the same tRNA molecule
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
Substrates: tRNATyr(GUA), tRNASer(AGA), and tRNAIle(UAU) are used to test the formation of m5C48
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?
S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
Substrates: yeast tRNASer(AGE)
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Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAHis
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAHis
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAHis
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAHis
-
Substrates: purified tRNAHis, secondary structure of mature Saccharomyces cerevisiae tRNAHis, overview
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAHis
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAHis
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNALeu(CAA)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALeu(CAA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNALeu(CAA)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALeu(CAA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNALeu(CAA)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALeu(CAA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
-
Substrates: yeast tRNA(GAA)
Products: -
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?
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
-
Substrates: yeast tRNA(GAA)
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
Substrates: the enzyme is responsible for complete m5C methylation of yeast tRNA. The frequency of modification depends on the cytosine position in tRNA. At positions 34 and 40, m5C is found only in two yeast tRNAs (tRNALeu (CUA) and tRNAPhe (GAA), respectively), whereas most other elongator yeast tRNAs bear either m5C48 or m5C49, but never both in the same tRNA molecule
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
Substrates: tRNAPhe(GAA) and tRNAAsp(GUC) are used to test the formation of m5C49
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S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
Substrates: yeast tRNAAsp(GUC)
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S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
-
Substrates: -
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Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAHis
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAHis
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAHis
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAHis
-
Substrates: purified tRNAHis, secondary structure of mature Saccharomyces cerevisiae tRNAHis, overview
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAHis
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAHis
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine72 in tRNACys
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNACys
Substrates: -
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S-adenosyl-L-methionine + cytosine72 in tRNACys
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNACys
Substrates: -
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Products: -
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S-adenosyl-L-methionine + cytosine72 in tRNACys
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNACys
Substrates: -
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S-adenosyl-L-methionine + cytosine72 in tRNACys
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNACys
Substrates: -
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S-adenosyl-L-methionine + cytosine72 in tRNACys
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNACys
Substrates: -
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S-adenosyl-L-methionine + cytosine72 in tRNACys
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNACys
Substrates: -
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S-adenosyl-L-methionine + cytosine72 in tRNACys
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNACys
Substrates: -
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S-adenosyl-L-methionine + cytosine72 in tRNAThr
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNAThr
Substrates: -
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S-adenosyl-L-methionine + cytosine72 in tRNAThr
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNAThr
Substrates: -
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S-adenosyl-L-methionine + cytosine72 in tRNAThr
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNAThr
Substrates: -
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S-adenosyl-L-methionine + cytosine72 in tRNAThr
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNAThr
Substrates: -
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S-adenosyl-L-methionine + cytosine72 in tRNAThr
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNAThr
Substrates: -
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S-adenosyl-L-methionine + cytosine72 in tRNAThr
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNAThr
Substrates: -
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S-adenosyl-L-methionine + cytosine72 in tRNAThr
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNAThr
Substrates: -
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additional information
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Substrates: identification of single-nucleotide resolution of cytosine 5-methylation sites in non-coding ribosomal RNAs and transfer RNAs of all three subcellular transcriptomes across six diverse species, overview. The enzyme does not methylate cytosines at structural positions C47, C48, C49 and C72. Identification of modified cytosines in Arabidopsis thaliana nuclear transcribed tRNAs which are dependent on RMTases TRDMT1 and TRM4B. No cytosine 5-methylation sites are detected in Arabidopsis chloroplast or mitochondrial tRNAs, which is in contrast to animal mitochondrial tRNAs
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additional information
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Substrates: motif I is essential for methyltransferase activity and is required for S-adenosyl-L-methionine binding and catalysis. Enzyme variant Trm4a is lacking motif I in contrast to enzyme variant Trm4b
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additional information
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Substrates: identification of single-nucleotide resolution of m5C sites in non-coding ribosomal RNAs and transfer RNAs of all three subcellular transcriptomes across six diverse species, overview
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additional information
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Substrates: identification of single-nucleotide resolution of m5C sites in non-coding ribosomal RNAs and transfer RNAs of all three subcellular transcriptomes across six diverse species, overview
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additional information
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Substrates: identification of single-nucleotide resolution of m5C sites in non-coding ribosomal RNAs and transfer RNAs of all three subcellular transcriptomes across six diverse species, overview
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additional information
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Substrates: NSUN2 candidate ncRNA targets identified include RNAs with central functions in the processing, folding and modification of other ncRNAs (RPPH1, Y RNA, SCARNA2), RNAs important for protein synthesis and trafficking (5S rRNA and 7SL RNA) and RNAs involved in multidrug resistance and other processes (Vault RNAs). Notably, all of the NSUN2 targets revealed by 5-azacytidine-mediated RNA immunoprecipitation are either transcribed by RNA Pol III in the nucleolus (SCARNA2 excepted), or function in the nucleolus (SCARNA2), where NSUN2 resides
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additional information
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Substrates: the iCLIP method identifies tRNA AspGTC, ValAAC, GlyGCC, and LeuCAA as methylation substrates with methylation within the variable arm at cytosines 48, 49, and 50, no additional NSun2 target sites outside the variable arm. vtRNAs are methylation substrates for NSun2, vtRNAs are ncRNAs found as part of the vault ribonucleoprotein complex
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additional information
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Substrates: development and evaluation of 5-azacytidine-mediated RNA immunoprecipitation, a mechanism-based technique in nine steps that exploits the covalent bond formed between an RNA methyltransferase and the cytidine analogue 5-azacytidine to recover RNA targets by immunoprecipitation, overview. The method enables over 200fold enrichment of tRNAs that are known targets of the enzyme revealing many tRNA and non-coding RNA targets not previously associated with NSUN2. High frequency of C>G transversions at the cytosine residues targeted by the enzyme, allowing identification of the specific methylated cytosine(s) in target RNAs. tRNAGly(GCC), bears four NSUN2 target sites (C40, 48, 49 and 50)
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additional information
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Substrates: development and evaluation of a customized version of the individual-nucleotide-resolution crosslinking and immunoprecipitation (iCLIP) method for detection of cytosine methylation in RNA species, site-specific methylation in tRNAs and additional messenger and noncoding RNAs (ncRNAs), overview. Identified NSun2 targets are tRNAs, mRNAs, and ncRNAs
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additional information
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Substrates: susbtrate specificity of NSUN6, overview. Three-dimensional L-shape structure of a tRNA with the positions of m5C modifications and the cognate methyltransferases responsible for installing them marked. The m5C modifications in cytoplasmic and mitochondrial tRNAs. Schematic secondary structure and three-dimensional L-shape structure of a tRNA with the positions of m5C modifications, determination of the interaction sites of NSUN6 with the discriminator base and additional base pairs in the acceptor stem and the D-loop, as observed by X-ray crystallography, overview. m5C72 modifications installed by NSUN6 lie within the acceptor stem of tRNA. NSUN6 forms extensive contacts with its substrate tRNAs. Binding of NSUN6 disrupts base pairing within the tRNA acceptor stem and promotes base-flipping of C71 to make the C5 atom of the C72 nucleotide, which is normally base paired with G1, accessible for methylation. NSUN6 also has a PUA domain that binds to the D-stem region of substrate tRNAs, as well as the non-genomically encoded CCA 3' end. Consistent with this binding mode, the presence of the CCA is found to be an essential pre-requisite for methylation of tRNACys and tRNAThr by NUSN6
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additional information
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Substrates: susbtrate specificity of NSUN6, overview. Three-dimensional L-shape structure of a tRNA with the positions of m5C modifications and the cognate methyltransferases responsible for installing them marked. The m5C modifications in cytoplasmic and mitochondrial tRNAs. Schematic secondary structure and three-dimensional L-shape structure of a tRNA with the positions of m5C modifications, determination of the interaction sites of NSUN6 with the discriminator base and additional base pairs in the acceptor stem and the D-loop, as observed by X-ray crystallography, overview. m5C72 modifications installed by NSUN6 lie within the acceptor stem of tRNA. NSUN6 forms extensive contacts with its substrate tRNAs. Binding of NSUN6 disrupts base pairing within the tRNA acceptor stem and promotes base-flipping of C71 to make the C5 atom of the C72 nucleotide, which is normally base paired with G1, accessible for methylation. NSUN6 also has a PUA domain that binds to the D-stem region of substrate tRNAs, as well as the non-genomically encoded CCA 3' end. Consistent with this binding mode, the presence of the CCA is found to be an essential pre-requisite for methylation of tRNACys and tRNAThr by NUSN6
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additional information
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Substrates: the CCA end is precisely recognized by hNSun6 primarily through the PUA domain, overview. The main chains of the residues (Arg126, Pro206 and Asp209) recognizes C74. Recognition for C75 comes from the main chain residues (Lys192 and Gly193) and the side chain residues (Lys192 and Asp209). The base moiety of C75 is stacked with the Tyr131 residue. Recognition for A76 is achieved mostly by the main chain of His129 and the side chain of Lys 192. Hydrophobic interactions with ambient aa residues, including Cys120, facilitate localization of the A76 base moiety. The discriminator base U73 binds to the RRM motif. C72 is recognized by the catalytic core. Multiple roles of the PUA domain in tRNA binding
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additional information
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Substrates: the CCA end is precisely recognized by hNSun6 primarily through the PUA domain, overview. The main chains of the residues (Arg126, Pro206 and Asp209) recognizes C74. Recognition for C75 comes from the main chain residues (Lys192 and Gly193) and the side chain residues (Lys192 and Asp209). The base moiety of C75 is stacked with the Tyr131 residue. Recognition for A76 is achieved mostly by the main chain of His129 and the side chain of Lys 192. Hydrophobic interactions with ambient aa residues, including Cys120, facilitate localization of the A76 base moiety. The discriminator base U73 binds to the RRM motif. C72 is recognized by the catalytic core. Multiple roles of the PUA domain in tRNA binding
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additional information
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Substrates: susbtrate specificity of NSUN2, overview. NSUN2 has a much broader target spectrum and is able to modify several positions (C34, C40, C48, C49, and C50) in a number of different tRNAs, as well as other RNA substrates. The enzyme is also active with various mRNAs. M5C modifications in cytoplasmic and mitochondrial tRNAs. Three-dimensional L-shape structure of a tRNA with the positions of m5C modifications and the cognate methyltransferases responsible for installing them marked. The m5C modifications in cytoplasmic and mitochondrial tRNAs. Schematic secondary structure and three-dimensional L-shape structure of a tRNA with the positions of m5C modifications. The broad-spectrum methyltransferase NSUN2 has been suggested to recognize different features in its diverse substrate RNAs. The reported NSUN2-mediated m5C modifications in mRNAs typically lie within highly GC-rich regions, suggesting that the enzyme may preferentially bind such sequences. But all the known NSUN2-mediated m5C modifications in vtRNAs lie within a UCG motif, and mutagenic analysis of the NSUN2 target pre-tRNALeu reveals a consensus sequence of C/A/U32-U/A33-m5C34-A35-A36-G37
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additional information
?
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Substrates: susbtrate specificity of NSUN2, overview. NSUN2 has a much broader target spectrum and is able to modify several positions (C34, C40, C48, C49, and C50) in a number of different tRNAs, as well as other RNA substrates. The enzyme is also active with various mRNAs. M5C modifications in cytoplasmic and mitochondrial tRNAs. Three-dimensional L-shape structure of a tRNA with the positions of m5C modifications and the cognate methyltransferases responsible for installing them marked. The m5C modifications in cytoplasmic and mitochondrial tRNAs. Schematic secondary structure and three-dimensional L-shape structure of a tRNA with the positions of m5C modifications. The broad-spectrum methyltransferase NSUN2 has been suggested to recognize different features in its diverse substrate RNAs. The reported NSUN2-mediated m5C modifications in mRNAs typically lie within highly GC-rich regions, suggesting that the enzyme may preferentially bind such sequences. But all the known NSUN2-mediated m5C modifications in vtRNAs lie within a UCG motif, and mutagenic analysis of the NSUN2 target pre-tRNALeu reveals a consensus sequence of C/A/U32-U/A33-m5C34-A35-A36-G37
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?
additional information
?
-
-
Substrates: highly conserved residues form a large, positively charged surface, which seems to be suitable for tRNA binding. Substrate specificity and methylation sites on tRNA, overview
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Products: -
?
additional information
?
-
-
Substrates: identification of single-nucleotide resolution of m5C sites in non-coding ribosomal RNAs and transfer RNAs of all three subcellular transcriptomes across six diverse species, overview
Products: -
Products: -
?
additional information
?
-
Substrates: susbtrate specificity of NSUN6, overview
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Products: -
?
additional information
?
-
Substrates: susbtrate specificity of NSUN6, overview
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Products: -
?
additional information
?
-
Substrates: susbtrate specificity of NSUN6, overview
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?
additional information
?
-
Substrates: susbtrate specificity of NSUN6, overview
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Products: -
?
additional information
?
-
Substrates: susbtrate specificity of NSUN6, overview
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Products: -
?
additional information
?
-
Substrates: susbtrate specificity of NSUN6, overview
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?
additional information
?
-
-
Substrates: a catalytic model for the RNA m5C methyltransferases that utilizes both conserved cysteines. The TC-Cys is proposed to perform covalent catalysis while the PC-Cys plays an important role in product release
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?
additional information
?
-
-
Substrates: Cys310 of motif VI is likely the nucleophilic catalyst of Trm4p
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additional information
?
-
-
Substrates: the enzyme Trm4 fabricate 5-methylcytosine (m5C) in RNA molecules utilizing a dual-cysteine catalytic mechanism
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additional information
?
-
-
Substrates: the enzyme forms covalent complexes with previously methylated RNA requiring S-adenosyl-L-homocysteine, the removal of this metabolite results in the disassembly of preexisting complexes
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?
additional information
?
-
Substrates: C34 methylation depends on Trm4a in both tRNALeuCAA and tRNAProCGG. Substrate specificity, comparison to trm4b, overview
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additional information
?
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Substrates: C34 methylation depends on Trm4a in both tRNALeuCAA and tRNAProCGG. Substrate specificity, comparison to trm4b, overview
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?
additional information
?
-
Substrates: Trm4b is active on the wild-type tRNA, its activity is slightly enhanced on C34A and completely abrogated on C49A, indicating that Trm4b has in vitro activity on tRNAProCGG and is specific for C49, which is in agreement with in vivo methylation data. Substrate specificity, comparison to trm4a, overview
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?
additional information
?
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Substrates: Trm4b is active on the wild-type tRNA, its activity is slightly enhanced on C34A and completely abrogated on C49A, indicating that Trm4b has in vitro activity on tRNAProCGG and is specific for C49, which is in agreement with in vivo methylation data. Substrate specificity, comparison to trm4a, overview
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?
additional information
?
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Substrates: C34 methylation depends on Trm4a in both tRNALeuCAA and tRNAProCGG. Substrate specificity, comparison to trm4b, overview
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?
additional information
?
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Substrates: C34 methylation depends on Trm4a in both tRNALeuCAA and tRNAProCGG. Substrate specificity, comparison to trm4b, overview
Products: -
Products: -
?
additional information
?
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Substrates: Trm4b is active on the wild-type tRNA, its activity is slightly enhanced on C34A and completely abrogated on C49A, indicating that Trm4b has in vitro activity on tRNAProCGG and is specific for C49, which is in agreement with in vivo methylation data. Substrate specificity, comparison to trm4a, overview
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?
additional information
?
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Substrates: Trm4b is active on the wild-type tRNA, its activity is slightly enhanced on C34A and completely abrogated on C49A, indicating that Trm4b has in vitro activity on tRNAProCGG and is specific for C49, which is in agreement with in vivo methylation data. Substrate specificity, comparison to trm4a, overview
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?
additional information
?
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Substrates: C34 methylation depends on Trm4a in both tRNALeuCAA and tRNAProCGG. Substrate specificity, comparison to trm4b, overview
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?
additional information
?
-
Substrates: C34 methylation depends on Trm4a in both tRNALeuCAA and tRNAProCGG. Substrate specificity, comparison to trm4b, overview
Products: -
Products: -
?
additional information
?
-
Substrates: Trm4b is active on the wild-type tRNA, its activity is slightly enhanced on C34A and completely abrogated on C49A, indicating that Trm4b has in vitro activity on tRNAProCGG and is specific for C49, which is in agreement with in vivo methylation data. Substrate specificity, comparison to trm4a, overview
Products: -
Products: -
?
additional information
?
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Substrates: Trm4b is active on the wild-type tRNA, its activity is slightly enhanced on C34A and completely abrogated on C49A, indicating that Trm4b has in vitro activity on tRNAProCGG and is specific for C49, which is in agreement with in vivo methylation data. Substrate specificity, comparison to trm4a, overview
Products: -
Products: -
?
additional information
?
-
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Substrates: identification of single-nucleotide resolution of m5C sites in non-coding ribosomal RNAs and transfer RNAs of all three subcellular transcriptomes across six diverse species, overview
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + cytosine in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine in tRNA precursor
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine15 in vtRNA1.3
S-adenosyl-L-homocysteine + 5-methylcytosine15 in vtRNA1.3
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine27 in vtRNA1.2
S-adenosyl-L-homocysteine + 5-methylcytosine27 in vtRNA1.2
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine27 in vtRNA1.3
S-adenosyl-L-homocysteine + 5-methylcytosine27 in vtRNA1.3
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA
S-adenosyl-L-methionine + cytosine34 in tRNALeu precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNALeu precursor
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNAPro(CGG)
S-adenosyl-L-methionine + cytosine4( in tRNAPro(AGG)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAPro(AGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine40 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA
S-adenosyl-L-methionine + cytosine40 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA precursor
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine40 in tRNAGly precursor
S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNAGly precursor
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
S-adenosyl-L-methionine + cytosine48 in tRNAAla(AGC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAAla(AGC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAAla(CGC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAAla(CGC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAAla(UGC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAAla(UGC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAAsp precursor
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAAsp precursor
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAAsp(GUC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAAsp(GUC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAAspGTC
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAAspGTC
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAGln(CUG)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAGln(CUG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAGln(UUG)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAGln(UUG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAGlu(CUC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAGlu(CUC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAGlu(UUC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAGlu(UUC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAGly precursor
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAGly precursor
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAGly(CCC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAGly(CCC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAGly(GCC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAGly(GCC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAGly(UCC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAGly(UCC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAGlyGCC
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAGlyGCC
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAHis
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAHis
S-adenosyl-L-methionine + cytosine48 in tRNAHis(GUG)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAHis(GUG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAIle(AAU)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAIle(AAU)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNALeu(AAG)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALeu(AAG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNALeu(CAA)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALeu(CAA)
S-adenosyl-L-methionine + cytosine48 in tRNALeu(CAA) precursor
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALeu(CAA) precursor
Substrates: NSUN2-mediated methylation of C34 of tRNALeu(CAA) has been shown to occur exclusively on intron-containing tRNA precursors
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNALeu(CAG)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALeu(CAG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNALeu(UAA)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALeu(UAA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNALeu(UAG)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALeu(UAG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNALeuCAA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALeuCAA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNALys(CUU)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALys(CUU)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNALys(UUU)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALys(UUU)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAMet(CAU)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAMet(CAU)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAPhe(GAA)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAPhe(GAA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAPro(UGG)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAPro(UGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNASer(AGA)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNASer(AGA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNASer(CGA)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNASer(CGA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNASer(GCU)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNASer(GCU)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNASer(UGA)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNASer(UGA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAThr(AGU)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAThr(AGU)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAThr(CGT)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAThr(CGT)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAThr(UGU)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAThr(UGU)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNATyr(GUA)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNATyr(GUA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAVal(AAC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAVal(AAC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAVal(CAC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAVal(CAC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNAVal(UAC)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAVal(UAC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
S-adenosyl-L-methionine + cytosine49 in tRNAasp precursor
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAAsp precursor
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAAsp(GUC)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAAsp(GUC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAAspGTC
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAAspGTC
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAGln(CUG)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAGln(CUG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAGln(UUG)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAGln(UUG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAGlu(CUC)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAGlu(CUC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAGlu(UUC)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAGlu(UUC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAGly precursor
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAGly precursor
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAGly(CCC)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAGly(CCC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAGly(GCC)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAGly(GCC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAGly(UCC)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAGly(UCC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAGlyGCC
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAGlyGCC
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNALeuCAA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNALeuCAA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNALys(UUU)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNALys(UUU)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAPhe(GAA)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAPhe(GAA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAPro(AGG)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAPro(AGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAPro(CGG)
S-adenosyl-L-methionine + cytosine49 in tRNAPro(UGG)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAPro(UGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAThr(AGU)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAThr(AGU)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAVal(AAC)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAVal(AAC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAVal(CAC)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAVal(CAC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAVal(UAC)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAVal(UAC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNA
S-adenosyl-L-methionine + cytosine50 in tRNAAspGTC
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAAspGTC
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAGlu(CUC)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAGlu(CUC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAGlu(UUC)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAGlu(UUC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAGly precursor
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAGly precursor
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAGly(CCC)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAGly(CCC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAGly(GCC)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAGly(GCC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAGly(UCC)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAGly(UCC)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAGlyGCC
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAGlyGCC
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAHis
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAHis
S-adenosyl-L-methionine + cytosine50 in tRNALeuCAA
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNALeuCAA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAPro(AGG)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAPro(AGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAPro(CGG)
S-adenosyl-L-methionine + cytosine50 in tRNAPro(UGG)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAPro(UGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine59 in vtRNA1.2
S-adenosyl-L-homocysteine + 5-methylcytosine59 in vtRNA1.2
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine59 in vtRNA1.3
S-adenosyl-L-homocysteine + 5-methylcytosine59 in vtRNA1.3
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine69 in vtRNA1.1
S-adenosyl-L-homocysteine + 5-methylcytosine69 in vtRNA1.1
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine72 in tRNACys
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNACys
S-adenosyl-L-methionine + cytosine72 in tRNACys(GCA)
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNACys(GCA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine72 in tRNAThr
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNAThr
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA
Substrates: the enzyme is responsible for complete m5C methylation of yeast tRNA. The frequency of modification depends on the cytosine position in tRNA. At positions 34 and 40, m5C is found only in two yeast tRNAs (tRNALeu (CUA) and tRNAPhe (GAA), respectively), whereas most other elongator yeast tRNAs bear either m5C48 or m5C49, but never both in the same tRNA molecule
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA
-
Substrates: cf. EC 2.1.1.203
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA
-
Substrates: cf. EC 2.1.1.203
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine34 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine40 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine40 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA
Substrates: the enzyme is responsible for complete m5C methylation of yeast tRNA. The frequency of modification depends on the cytosine position in tRNA. At positions 34 and 40, m5C is found only in two yeast tRNAs (tRNALeu (CUA) and tRNAPhe (GAA), respectively), whereas most other elongator yeast tRNAs bear either m5C48 or m5C49, but never both in the same tRNA molecule
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine40 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine40 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
-
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
Substrates: the enzyme is responsible for complete m5C methylation of yeast tRNA. The frequency of modification depends on the cytosine position in tRNA. At positions 34 and 40, m5C is found only in two yeast tRNAs (tRNALeu (CUA) and tRNAPhe (GAA), respectively), whereas most other elongator yeast tRNAs bear either m5C48 or m5C49, but never both in the same tRNA molecule
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
-
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
-
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
Substrates: -
Products: -
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S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
Substrates: -
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S-adenosyl-L-methionine + cytosine48 in tRNAHis
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAHis
-
Substrates: -
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S-adenosyl-L-methionine + cytosine48 in tRNAHis
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAHis
-
Substrates: -
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?
S-adenosyl-L-methionine + cytosine48 in tRNALeu(CAA)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALeu(CAA)
Substrates: -
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S-adenosyl-L-methionine + cytosine48 in tRNALeu(CAA)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALeu(CAA)
Substrates: -
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Products: -
?
S-adenosyl-L-methionine + cytosine48 in tRNALeu(CAA)
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNALeu(CAA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
Substrates: the enzyme is responsible for complete m5C methylation of yeast tRNA. The frequency of modification depends on the cytosine position in tRNA. At positions 34 and 40, m5C is found only in two yeast tRNAs (tRNALeu (CUA) and tRNAPhe (GAA), respectively), whereas most other elongator yeast tRNAs bear either m5C48 or m5C49, but never both in the same tRNA molecule
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
Substrates: -
Products: -
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?
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
Substrates: -
Products: -
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?
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
Substrates: -
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?
S-adenosyl-L-methionine + cytosine49 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAPro(CGG)
Substrates: -
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?
S-adenosyl-L-methionine + cytosine49 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAPro(CGG)
Substrates: -
Products: -
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?
S-adenosyl-L-methionine + cytosine49 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine49 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNA
Substrates: -
Products: -
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?
S-adenosyl-L-methionine + cytosine50 in tRNAHis
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAHis
-
Substrates: -
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?
S-adenosyl-L-methionine + cytosine50 in tRNAHis
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAHis
-
Substrates: -
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Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine50 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine72 in tRNACys
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNACys
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine72 in tRNACys
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNACys
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine72 in tRNACys
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNACys
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine72 in tRNACys
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNACys
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine72 in tRNACys
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNACys
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine72 in tRNACys
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNACys
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine72 in tRNACys
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNACys
Substrates: -
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Products: -
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S-adenosyl-L-methionine + cytosine72 in tRNAThr
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNAThr
Substrates: -
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?
S-adenosyl-L-methionine + cytosine72 in tRNAThr
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNAThr
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine72 in tRNAThr
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNAThr
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine72 in tRNAThr
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNAThr
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine72 in tRNAThr
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNAThr
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine72 in tRNAThr
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNAThr
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine72 in tRNAThr
S-adenosyl-L-homocysteine + 5-methylcytosine72 in tRNAThr
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: identification of single-nucleotide resolution of cytosine 5-methylation sites in non-coding ribosomal RNAs and transfer RNAs of all three subcellular transcriptomes across six diverse species, overview. The enzyme does not methylate cytosines at structural positions C47, C48, C49 and C72. Identification of modified cytosines in Arabidopsis thaliana nuclear transcribed tRNAs which are dependent on RMTases TRDMT1 and TRM4B. No cytosine 5-methylation sites are detected in Arabidopsis chloroplast or mitochondrial tRNAs, which is in contrast to animal mitochondrial tRNAs
Products: -
Products: -
?
additional information
?
-
-
Substrates: identification of single-nucleotide resolution of m5C sites in non-coding ribosomal RNAs and transfer RNAs of all three subcellular transcriptomes across six diverse species, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: identification of single-nucleotide resolution of m5C sites in non-coding ribosomal RNAs and transfer RNAs of all three subcellular transcriptomes across six diverse species, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: identification of single-nucleotide resolution of m5C sites in non-coding ribosomal RNAs and transfer RNAs of all three subcellular transcriptomes across six diverse species, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: NSUN2 candidate ncRNA targets identified include RNAs with central functions in the processing, folding and modification of other ncRNAs (RPPH1, Y RNA, SCARNA2), RNAs important for protein synthesis and trafficking (5S rRNA and 7SL RNA) and RNAs involved in multidrug resistance and other processes (Vault RNAs). Notably, all of the NSUN2 targets revealed by 5-azacytidine-mediated RNA immunoprecipitation are either transcribed by RNA Pol III in the nucleolus (SCARNA2 excepted), or function in the nucleolus (SCARNA2), where NSUN2 resides
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additional information
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-
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Substrates: the iCLIP method identifies tRNA AspGTC, ValAAC, GlyGCC, and LeuCAA as methylation substrates with methylation within the variable arm at cytosines 48, 49, and 50, no additional NSun2 target sites outside the variable arm. vtRNAs are methylation substrates for NSun2, vtRNAs are ncRNAs found as part of the vault ribonucleoprotein complex
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additional information
?
-
-
Substrates: identification of single-nucleotide resolution of m5C sites in non-coding ribosomal RNAs and transfer RNAs of all three subcellular transcriptomes across six diverse species, overview
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additional information
?
-
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Substrates: the enzyme Trm4 fabricate 5-methylcytosine (m5C) in RNA molecules utilizing a dual-cysteine catalytic mechanism
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additional information
?
-
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Substrates: identification of single-nucleotide resolution of m5C sites in non-coding ribosomal RNAs and transfer RNAs of all three subcellular transcriptomes across six diverse species, overview
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the S-adenosyl-L-methionine analigue sinefungin is bound in a negatively charged pocket near helix alpha8, binding structure, detailed overview
-
S-adenosyl-L-methionine
-
helix alpha8 can adopt two different conformations, thereby controlling the entry of S-adenosyl-L-methionine into the active site
S-adenosyl-L-methionine
cofactor interacting residues in hNSun6 are mainly composed of conserved residues Leu241, Cys242, Pro325 and Leu354. In addition, the side chain of residue Asp293 recognizes the N6 of the adenine ring. Asp293 is conserved as Asp or Glu in the RNA:m5C MTase family
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-aza-2'-deoxycytidine
-
the catalytic mechanism is disrupted by the suicide inhibitor
additional information
structure-based drug design toward RNA:m5C methyltransferase-related diseases
-
additional information
-
structure-based drug design toward RNA:m5C methyltransferase-related diseases
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
levels of tRNAHis m5C increase following several nutrient starvation treatments of the BY4741 strain, Trm4 protein levels do not increase during starvation conditions
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinogenesis
Depletion of TRDMT1 affects 5-methylcytosine modification of mRNA and inhibits HEK293 cell proliferation and migration.
Carcinogenesis
m5C-Related Signatures for Predicting Prognosis in Cutaneous Melanoma with Machine Learning.
Carcinoma
NOP2/Sun RNA methyltransferase 2 promotes tumor progression via its interacting partner RPL6 in gallbladder carcinoma.
Glioma
Identification of RNA: 5-Methylcytosine Methyltransferases-Related Signature for Predicting Prognosis in Glioma.
Leukemia
Trdmt1 3'-untranslated region functions as a competing endogenous RNA in leukemia HL-60 cell differentiation.
Microcephaly
Aberrant methylation of tRNAs links cellular stress to neuro-developmental disorders.
Neoplasms
High expression of NSUN5 promotes cell proliferation via cell cycle regulation in colorectal cancer.
Neoplasms
m5C modification of mRNA serves a DNA damage code to promote homologous recombination.
Neoplasms
NOP2/Sun RNA methyltransferase 2 promotes tumor progression via its interacting partner RPL6 in gallbladder carcinoma.
Neoplasms
The RNA methyltransferase NSUN6 suppresses pancreatic cancer development by regulating cell proliferation.
Neoplasms
Ubiquitination-mediated degradation of TRDMT1 regulates homologous recombination and therapeutic response.
Ovarian Neoplasms
Ubiquitination-mediated degradation of TRDMT1 regulates homologous recombination and therapeutic response.
Pancreatic Neoplasms
The RNA methyltransferase NSUN6 suppresses pancreatic cancer development by regulating cell proliferation.
Primary Ovarian Insufficiency
TRDMT1 participates in the DNA damage repair of granulosa cells in premature ovarian failure.
Spinal Dysraphism
An association study of 45 folate-related genes in spina bifida: Involvement of cubilin (CUBN) and tRNA aspartic acid methyltransferase 1 (TRDMT1).
Squamous Cell Carcinoma of Head and Neck
Gene signatures of m5C regulators may predict prognoses of patients with head and neck squamous cell carcinoma.
Tetralogy of Fallot
Mutations in RNA Methyltransferase Gene NSUN5 Confer High Risk of Outflow Tract Malformation.
Williams Syndrome
Expression of the RNA methyltransferase Nsun5 is essential for developing cerebral cortex.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady-state kinetic analyses of the methylation of m5Cprobe, tRNA and ssRNA by NSUN2
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 6.5
-
maximal formation of Trm4p-RNA complexes observed in the pH range of 5.5-6.5
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
neuroepithelial-like stem cells derived from pluripotent cells
brenda
reduction of upper-layer neurons in the Nsun2 -/- cortex, mouse brain cortex at E18.5 showing the location of the indicated markers
brenda
-
slightly increasing trend of m5C modification in mRNA from 3- to 15-day-old whole seedlings undergoing vegetative, floral transitional, and reproductive stages
brenda
additional information
NSUN2 is expressed in stem and progenitor cells during human brain development
brenda
expression of NSUN2 during human neural differentiation, overview
brenda
additional information
-
transcriptome-wide profiling of m5C RNA in Arabidopsis thaliana is made by applying m5C RNA immunoprecipitation followed by a deepsequencing approach (m5C-RIP-seq). LC-MS/MS and dot blot analyses reveal a dynamic pattern of m5C mRNA modification in various tissues and at different developmental stages. m5C-RIP-seq analysis identified 6045m5C peaks in 4465 expressed genes in young seedlings. m5C is enriched in coding sequences with two peaks located immediately after start codons and before stop codons, and is associated with mRNAs with low translation activity. Spatial change in m5C levels in different tissues
brenda
additional information
NSUN2 is overexpressed in a number of human cancers
brenda
additional information
NSUN2 is expressed in early neuroepithelial progenitors of the developing human brain, and its expression is gradually reduced during differentiation of human neuroepithelial stem (NES) cells in vitro. Nucleolar expression of NSUN2 overlaps with SOX1, a marker for early neuroepithelial progenitors in the neural tube. NSUN2 is expressed in early neuroectodermal cells that are capable of differentiating into various region-specific neuronal and glial cell types. NSUN2 co-localized with Nestin and SOX1 in cultured NES cells, both lines Sai1 and AF22 express high levels of the NES cell markers Nestin and SOX2 but very low levels of the neural differentiation marker betaIII-tubulin (TUBB3)
brenda
additional information
nucleolar expression of NSUN2 overlaps with SOX1, a marker for early neuroepithelial progenitors in the neural tube. NSUN2 is expressed in early neuroectodermal cells that are capable of differentiating into various region-specific neuronal and glial cell types
brenda
additional information
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tRNAHis m5C levels are unusually responsive to yeast growth conditions
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
enzyme NSUN6 localizes to the cytoplasm and appears enriched in proximity to the golgi aparatus and pericentriolar matrix, indicating that methylation of C72 residues is a late maturation event that takes place after nuclear export
-
brenda
additional information
enzyme NSUN6 localizes to the cytoplasm and appears enriched in proximity to the golgi aparatus and pericentriolar matrix, indicating that methylation of C72 residues is a late maturation event that takes place after nuclear export
-
brenda
additional information
NSUN2 localizes predominantly in the nucleus
-
brenda
additional information
NSUN2 localizes predominantly in the nucleus
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
the enzyme belongs to the RsmF/YebU/NSUN2 family of cytosine 5-methylation-RNA methyltransferases utilizing two cysteines in their catalytic pocket
evolution
-
both the nucleotide position and percent methylation of tRNAs and rRNAs m5C sites were conserved across all species analysed
evolution
-
both the nucleotide position and percent methylation of tRNAs and rRNAs m5C sites are conserved across all species analysed
evolution
-
Identification of m5C sites in nuclear, chloroplast and mitochondrial tRNAs. 39 cytosine 5-methylation sites are identified at 5 structural positions and are located in tRNA secondary structure at positions C38, C48, C49, C50 and C72, pattern of methylation in individual tRNA isodecoders, overview. Identification of single-nucleotide resolution of cytosine 5-methylation sites in non-coding ribosomal RNAs and transfer RNAs of all three subcellular transcriptomes across six diverse species. Both the nucleotide position and percent methylation of tRNAs and rRNAs cytosine 5-methylation sites are conserved across all species analysed, overview
evolution
-
both the nucleotide position and percent methylation of tRNAs and rRNAs m5C sites are conserved across all species analysed, overview
evolution
-
both the nucleotide position and percent methylation of tRNAs and rRNAs m5C sites were conserved across all species analysed
evolution
-
both the nucleotide position and percent methylation of tRNAs and rRNAs m5C sites are conserved across all species analysed, overview
evolution
phylogenetic tree of Trm4/ NSun2 homologues, overview. In contrast to most other organisms, fission yeast Schizosaccharomyces pombe carries two Trm4/NSun2 homologues, Trm4a (SPAC17D4.04) and Trm4b (SPAC23C4.17). Enzyme Trm4a is responsible for in vivo methylation of C34 and C48 methylation, whereas Trm4b methylates C49 and C50, tRNAProCGG is the only tRNA methylated by both Trm4a and Trm4b. Schizosaccharomyces pombe shows an unusual separation of activities of the NSun2/Trm4 enzymes that are united in a single enzyme in other eukaryotes like humans, mice and Saccharomyces cerevisiae
evolution
phylogenetic tree of Trm4/ NSun2 homologues, overview. Enzyme Trm4a is responsible for in vivo methylation of C34 and C48 methylation, whereas Trm4b methylates C49 and C50, tRNAProCGG is the only tRNA methylated by both Trm4a and Trm4b. Schizosaccharomyces pombe shows an unusual separation of activities of the NSun2/Trm4 enzymes that are united in a single enzyme in other eukaryotes like humans, mice and Saccharomyces cerevisiae
evolution
-
phylogenetic tree of Trm4/ NSun2 homologues, overview. In contrast to most other organisms, fission yeast Schizosaccharomyces pombe carries two Trm4/NSun2 homologues, Trm4a (SPAC17D4.04) and Trm4b (SPAC23C4.17). Enzyme Trm4a is responsible for in vivo methylation of C34 and C48 methylation, whereas Trm4b methylates C49 and C50, tRNAProCGG is the only tRNA methylated by both Trm4a and Trm4b. Schizosaccharomyces pombe shows an unusual separation of activities of the NSun2/Trm4 enzymes that are united in a single enzyme in other eukaryotes like humans, mice and Saccharomyces cerevisiae
-
evolution
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phylogenetic tree of Trm4/ NSun2 homologues, overview. Enzyme Trm4a is responsible for in vivo methylation of C34 and C48 methylation, whereas Trm4b methylates C49 and C50, tRNAProCGG is the only tRNA methylated by both Trm4a and Trm4b. Schizosaccharomyces pombe shows an unusual separation of activities of the NSun2/Trm4 enzymes that are united in a single enzyme in other eukaryotes like humans, mice and Saccharomyces cerevisiae
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evolution
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phylogenetic tree of Trm4/ NSun2 homologues, overview. In contrast to most other organisms, fission yeast Schizosaccharomyces pombe carries two Trm4/NSun2 homologues, Trm4a (SPAC17D4.04) and Trm4b (SPAC23C4.17). Enzyme Trm4a is responsible for in vivo methylation of C34 and C48 methylation, whereas Trm4b methylates C49 and C50, tRNAProCGG is the only tRNA methylated by both Trm4a and Trm4b. Schizosaccharomyces pombe shows an unusual separation of activities of the NSun2/Trm4 enzymes that are united in a single enzyme in other eukaryotes like humans, mice and Saccharomyces cerevisiae
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evolution
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phylogenetic tree of Trm4/ NSun2 homologues, overview. Enzyme Trm4a is responsible for in vivo methylation of C34 and C48 methylation, whereas Trm4b methylates C49 and C50, tRNAProCGG is the only tRNA methylated by both Trm4a and Trm4b. Schizosaccharomyces pombe shows an unusual separation of activities of the NSun2/Trm4 enzymes that are united in a single enzyme in other eukaryotes like humans, mice and Saccharomyces cerevisiae
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malfunction
disruption of the ORF YBL024w leads to the complete absence of m5C in total yeast tRNA. No tRNA:m5C-methyltransferase activity towards all potential m5C methylation sites is detected in the extract of the disrupted yeast strain. The protein product of a single gene is responsible for complete m5C methylation of yeast tRNA
malfunction
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NSUN2 is associated with Myc-induced proliferation of cancer cells, mitotic spindle stability, infertility in male mice, and the balance of selfrenewal and differentiation in skin stem cells. In humans NSUN2 mutations cause an autosomal recessive syndrome characterized by intellectual disability and mental retardation
malfunction
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in trm4a defective mutants, the cytosine 5-methylation profile is the same as wild-type, showing that TRM4A is not required for methylation of any of the detected tRNAs. In contrast for trm4b-1 and trm4b-2 mutants, a total of 18 sites have no detectable methylation and 7 sites have reduced methylation when compared to wild-type, the sites are corresponding to structural positions C48, C49, and C50. trdmt1/trm4b double mutants are hypersensitive to the antibiotic hygromycin B
malfunction
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yeast strains depleted of tRNAHis guanylyltransferase accumulate uncharged tRNAHis lacking the G-1 residue and subsequently accumulate additional 5-methylcytidine (m5C) at residues C48 and C50 of tRNAHis, due to the activity of the m5Cmethyltransferase Trm4. The increase in tRNAHis m5C levels does not require loss of Thg1, loss of G-1 of tRNAHis, or cell death but is associated with growth arrest following different stress conditions. Substantially increased tRNAHis m5C levels occur after temperature-sensitive strains are grown at nonpermissive temperature, and after wild-type strains are grown to stationary phase, starved for required amino acids, or treated with rapamycin. More modest accumulations of m5C in tRNAHis occur after starvation for glucose and after starvation for uracil. In virtually all cases examined, the additional m5C on tRNAHis occurs while cells are fully viable, and the increase is neither due to the GCN4 pathway, nor to increased Trm4 levels, phenotypes, overview. The increased amount of m5C is specific to tRNAHis. tRNAVal(AAC), which also normally has unmodified C48 and C50 residues adjacent to m5C49, has only marginally increased levels of m5C 7 h after temperature shift in the fcp1-1ts mutant
malfunction
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autosomal-recessive loss of the NSUN2 gene is a causative link to intellectual disability disorders in humans. Loss of cytosine-5 methylation in vault RNAs causes aberrant processing into Argonaute-associated small RNA fragments that can function as microRNAs. Impaired processing of vault ncRNA may contribute to the etiology of NSun2-deficiency human disorders
malfunction
exposure to oxidative stress efficiently repressed NSUN2, causing a reduction of methylation at specific tRNA sites. Loss of NSUN2 alters the biogenesis of tRNA-derived noncoding fragments (tRFs) in response to stress, leading to impaired regulation of protein synthesis. The intracellular accumulation of a specific subset of tRFs correlates with the dynamic repression of global protein synthesis. Disruption of the Nsun2 gene in mice causes global hypomethylation of tRNAs and a developmental growth retardation. The abnormal development of tissues including brain and skin is the result of impaired stem cell differentiation. The expression of NSUN2 is highly dynamic within tissues. For instance, NSUN2 is absent in quiescent stem cells in hair follicle bulges (BGs), steadily increases in progenitor cells in the hair germ, and is highest in the growing (anagen) hair bulb
malfunction
exposure to oxidative stress efficiently repressed NSUN2, causing a reduction of methylation at specific tRNA sites. Loss of NSUN2 alters the biogenesis of tRNA-derived noncoding fragments (tRFs) in response to stress, leading to impaired regulation of protein synthesis. The intracellular accumulation of a specific subset of tRFs correlates with the dynamic repression of global protein synthesis
malfunction
loss-of-function mutations in the NSUN2 gene in both mouse and human cause growth retardation and neurodevelopmental deficits including microcephaly, as well as defects in cognition and motor function. Loss of NSUN2-mediated methylation of tRNA increases their endonucleolytic cleavage by angiogenin, and 5' tRNA fragments accumulate in Nsun2-/- brains. Neural differentiation of NES cells is impaired by both NSUN2 depletion and the presence of angiogenin. Since repression of NSUN2 also inhibits neural cell migration toward the chemoattractant fibroblast growth factor 2, the impaired differentiation capacity in the absence of NSUN2 may be driven by the inability to efficiently respond to growth factors. Upper-layer neurons are decreased in Nsun2 knockout brains, phenotype, detailed overview
malfunction
loss-of-function mutations in the NSUN2 gene in both mouse and human cause growth retardation and neurodevelopmental deficits including microcephaly, as well as defects in cognition and motor function. Loss of NSUN2-mediated methylation of tRNA increases their endonucleolytic cleavage by angiogenin, and 5' tRNA fragments accumulate in Nsun2-/- brains. Neural differentiation of NES cells is impaired by both NSUN2 depletion and the presence of angiogenin. Since repression of NSUN2 also inhibits neural cell migration toward the chemoattractant fibroblast growth factor 2, the impaired differentiation capacity in the absence of NSUN2 may be driven by the inability to efficiently respond to growth factors. Upper-layer neurons are decreased in Nsun2 knockout brains, phenotype, detailed overview. In the developing Nsun2-/- mouse cerebral cortex, intermediate progenitors accumulate and upper-layer neurons decrease. .Loss of NSUN2-mediated methylation of tRNA increases their endonucleolytic cleavage by angiogenin, and 5' tRNA fragments accumulate in Nsun2 -/- brains
malfunction
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mutations in TRM4B display defects in root development and decreased m5C peaks. TRM4B affects the transcript levels of the genes involved in root development, which is positively correlated with their mRNA stability and m5C levels
malfunction
the absence of Trm4a, but not Trm4b, causes a mild resistance of Schizosaccharomyces pombe to calcium chloride. In trm4aDELTA mutants, the C34 methylation level drops to background levels (8%), whereas C49 methylation remains at 82%. m5C34 is at 94% in trm4bDELTA mutant, and m5C49 drops to 9%, thus confirming that Trm4a is responsible for m5C34 and Trm4b for m5C49 on tRNAProCGG in vivo
malfunction
the absence of Trm4a, but not Trm4b, causes a mild resistance of Schizosaccharomyces pombe to calcium chloride. Absence of Trm4a, but not Trm4b, causes a mild resistance of Schizosaccharomyces pombe to calcium chloride. In trm4aDELTA mutants, the C34 methylation level drops to background levels (8%), whereas C49 methylation remains at 82%. m5C34 is at 94% in trm4bDELTA mutant, and m5C49 drops to 9%, thus confirming that Trm4a is responsible for m5C34 and Trm4b for m5C49 on tRNAProCGG in vivo
malfunction
tRNAs lacking m5C48/49/50 modifications are bound more tightly by angiogenin, leading to accumulation of 5' tRNA-derived small RNA fragments, which trigger cellular stress and are implicated in disease. Expression of catalytically inactive forms of NSUN2, but not NSUN1, NSUN5, or NSUN6, is reported to alter the total amount of m5C detected in the mRNA pool. svRNA4 acts analogously to a microRNA and a concomitant increase in the levels of the svRNA4 target mRNAs CACNG7 and CACNG8 is observed in NSUN2-/- cells. Loss of function mutations in NSUN2 underlie several neurodevelopmental disorders. A homozygous mutation in the NSUN2 gene that leads to the substitution of Gly679 for Arg (p.Gly679Arg) in the protein has been detected in individuals with autosomal-recessive intellectual disability. This amino acid substitution is suggested to impede NSUN2 function by preventing localization of the protein to its site of action in the nucleolus. NSUN2 has also been linked to Dubowitz syndrome, which is characterized by microcephaly, growth and mental retardation, eczema, and characteristic facial features. A homozygous mutation in the canonical splice acceptor of exon 6 leads to use of a cryptic splice donor, instability of the NSUN2 mRNA, a significant decrease in protein levels, and reduced methylation of NSUN2 target RNAs (m5C47/48 of tRNAAsp(GUC)
malfunction
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yeast strains depleted of tRNAHis guanylyltransferase accumulate uncharged tRNAHis lacking the G-1 residue and subsequently accumulate additional 5-methylcytidine (m5C) at residues C48 and C50 of tRNAHis, due to the activity of the m5Cmethyltransferase Trm4. The increase in tRNAHis m5C levels does not require loss of Thg1, loss of G-1 of tRNAHis, or cell death but is associated with growth arrest following different stress conditions. Substantially increased tRNAHis m5C levels occur after temperature-sensitive strains are grown at nonpermissive temperature, and after wild-type strains are grown to stationary phase, starved for required amino acids, or treated with rapamycin. More modest accumulations of m5C in tRNAHis occur after starvation for glucose and after starvation for uracil. In virtually all cases examined, the additional m5C on tRNAHis occurs while cells are fully viable, and the increase is neither due to the GCN4 pathway, nor to increased Trm4 levels, phenotypes, overview. The increased amount of m5C is specific to tRNAHis. tRNAVal(AAC), which also normally has unmodified C48 and C50 residues adjacent to m5C49, has only marginally increased levels of m5C 7 h after temperature shift in the fcp1-1ts mutant
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malfunction
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the absence of Trm4a, but not Trm4b, causes a mild resistance of Schizosaccharomyces pombe to calcium chloride. In trm4aDELTA mutants, the C34 methylation level drops to background levels (8%), whereas C49 methylation remains at 82%. m5C34 is at 94% in trm4bDELTA mutant, and m5C49 drops to 9%, thus confirming that Trm4a is responsible for m5C34 and Trm4b for m5C49 on tRNAProCGG in vivo
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malfunction
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the absence of Trm4a, but not Trm4b, causes a mild resistance of Schizosaccharomyces pombe to calcium chloride. Absence of Trm4a, but not Trm4b, causes a mild resistance of Schizosaccharomyces pombe to calcium chloride. In trm4aDELTA mutants, the C34 methylation level drops to background levels (8%), whereas C49 methylation remains at 82%. m5C34 is at 94% in trm4bDELTA mutant, and m5C49 drops to 9%, thus confirming that Trm4a is responsible for m5C34 and Trm4b for m5C49 on tRNAProCGG in vivo
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malfunction
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the absence of Trm4a, but not Trm4b, causes a mild resistance of Schizosaccharomyces pombe to calcium chloride. In trm4aDELTA mutants, the C34 methylation level drops to background levels (8%), whereas C49 methylation remains at 82%. m5C34 is at 94% in trm4bDELTA mutant, and m5C49 drops to 9%, thus confirming that Trm4a is responsible for m5C34 and Trm4b for m5C49 on tRNAProCGG in vivo
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malfunction
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the absence of Trm4a, but not Trm4b, causes a mild resistance of Schizosaccharomyces pombe to calcium chloride. Absence of Trm4a, but not Trm4b, causes a mild resistance of Schizosaccharomyces pombe to calcium chloride. In trm4aDELTA mutants, the C34 methylation level drops to background levels (8%), whereas C49 methylation remains at 82%. m5C34 is at 94% in trm4bDELTA mutant, and m5C49 drops to 9%, thus confirming that Trm4a is responsible for m5C34 and Trm4b for m5C49 on tRNAProCGG in vivo
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metabolism
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formation of a covalent complex between dual-cysteine RNA:m5C methyltransferases and methylated RNA provides a unique means by which metabolic factors can influence RNA. By controlling the degree of formation of the enzyme-RNA covalent complex, S-adenosyl-L-homocysteine and pH are likely to influence the extent of m5C formation and the rate of release of methylated RNA from RNA:m5C methyltransferases. Metabolite-induced covalent complexes could plausibly affect the processing and function of m5C-containing RNAs
metabolism
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the GCN4 pathway is not responsible for additional m5C levels on tRNAHis
metabolism
on a global level, depletion, overexpression, or expression of catalytically inactive forms of NSUN2, but not NSUN1, NSUN5, or NSUN6, is reported to alter the total amount of m5C detected in the mRNA pool. Roles of m5C RNA methyltransferases in development and disease, overview
metabolism
m5C methylation of RNA is catalysed by the NOL1/NOP2/Sun domain (NSUN) RNA methyltransferase family, which includes NSUN1-7, as well as the DNA MTase homologue TRDMT1 (formerly DNMT2)
metabolism
enzyme NSUN2 plays a central role in regulation of the stress response pathway, detailed overview. tRNAs play multiple regulatory roles in the adaptation of protein synthesis to the cellular stress response
metabolism
enzyme NSUN2 plays a central role in regulation of the stress respone pathway, detailed overview. tRNAs play multiple regulatory roles in the adaptation of protein synthesis to the cellular stress response
metabolism
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the GCN4 pathway is not responsible for additional m5C levels on tRNAHis
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physiological function
the enzyme is responsible for complete m5C methylation of yeast tRNA
physiological function
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post-transcriptional methylation of RNA cytosine residues to 5-methylcytosine (m5C) is an important modification that regulates RNA metabolism
physiological function
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post-transcriptional methylation of RNA cytosine residues to 5-methylcytosine (m5C) is an important modification that regulates RNA metabolism
physiological function
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post-transcriptional methylation of RNA cytosine residues to 5-methylcytosine is an important modification that regulates RNA metabolism. Nuclear tRNA methylation requires two evolutionarily conserved methyltransferases, TRDMT1 and TRM4B
physiological function
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post-transcriptional methylation of RNA cytosine residues to 5-methylcytosine (m5C) is an important modification that regulates RNA metabolism
physiological function
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post-transcriptional methylation of RNA cytosine residues to 5-methylcytosine (m5C) is an important modification that regulates RNA metabolism
physiological function
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post-transcriptional methylation of RNA cytosine residues to 5-methylcytosine (m5C) is an important modification that regulates RNA metabolism
physiological function
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no evidence for a major role of NSun2 or NSun2-mediated cytosine-5 methylation in mRNA stability
physiological function
cytoplasmic transfer RNAs are methylated by NSUN2, NSUN6, and DNMT2. NSUN6 specifically methylates C72 of particular tRNAs. U73, which has been termed the discriminator base, is critical for substrate recognition by NSUN6, and a flexible base pair (A:U or U:A) at positions 2:71 as well as a rigid base pair (C:G or G:C) formed between positions 3:70 are preferred. The binding pocket of human NSUN6 specifically accommodates U73. Roles of m5C RNA methyltransferases in development and disease, overview
physiological function
cytoplasmic transfer RNAs are methylated by NSUN2, NSUN6, and DNMT2. Structural differences in PhNSUN6 enable the archaeal enzyme to bind tRNAs containing either U73 or G73, thereby broadening its target spectrum compared to its human homologue enzyme, comparison of NSUN family enzymes, overview. The NSUN family enzymes use the cysteine located in amino acid motif VI for the nucleophilic attack on carbon 6 of the target cytosine in RNA. In all seven human NSUN variants, the catalytic cysteine is preceded by threonine. Hydrogen bonding with the backbone carbonyl of proline and the aspartate side chain in motif IV orients the base in the active site and assists bond formation by transient protonation of the endocyclic N3 of cytidine. The activated nucleobase then accepts a methyl group from the properly positioned SAM cofactor, resulting in the formation of a carbon-carbon bond and generation of S-adenosylhomocysteine (SAH). To complete the reaction, the covalently bound methylated RNA has to be released from the protein. This elimination is assisted by the cysteine located in motif IV of NSUN proteins. This cysteine is located next to the conserved proline and acts as a base to deprotonate the tetrahedral carbon and initiate the elimination reaction that restores the unsaturated m5C heterocycle. m5C72 is reported to promote the thermal stability of PhtRNAs. Roles of m5C RNA methyltransferases in development and disease, overview
physiological function
the cytosine-5 RNA methyltransferase NSUN2 is a sensor for external stress stimuli. NSUN2-driven RNA methylation is functionally required to adapt cell cycle progression to the early stress response. The nucleolus, where NSUN2 resides, can act as a stress sensor. Dynamic changes of site-specific Methylcytosine (m5C) levels require NSUN2. m5C is required to balance anabolic and catabolic pathways during the stress response
physiological function
the cytosine-5 RNA methyltransferase NSUN2 is a sensor for external stress stimuli. NSUN2-driven RNA methylation is functionally required to adapt cell cycle progression to the early stress response. The nucleolus, where NSUN2 resides, can act as a stress sensor. Dynamic changes of site-specific Methylcytosine (m5C) levels require NSUN2. m5C is required to balance anabolic and catabolic pathways during the stress response
physiological function
cytosine-5 methylation in RNA is mediated by a large protein family of conserved RNA:m5C-methyltransferases. NSUN2 is one member of this family and methylates the vast majority of tRNAs as well as a small number of other non-coding (ncRNAs) and coding RNAs (cRNAs). The correct deposition of m5C into RNAs is essential for normal development. Cytosine-5 RNA methylation regulates neural stem cell differentiation and motility. The correct deposition of m5C into RNAs is essential for normal development
physiological function
cytosine-5 methylation in RNA is mediated by a large protein family of conserved RNA:m5C-methyltransferases. NSUN2 is one member of this family and methylates the vast majority of tRNAs as well as a small number of other non-coding (ncRNAs) and coding RNAs (cRNAs). The correct deposition of m5C into RNAs is essential for normal development. Cytosine-5 RNA methylation regulates neural stem cell differentiation and motility. The correct deposition of m5C into RNAs is essential for normal development
physiological function
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TRM4B encodes a potential mRNA m5C methyltransferase (RCMT). 5-methylcytosine (m5C) is a DNA modification predominantly reported in abundant non-coding RNAs in both prokaryotes and eukaryotes. tRNA-specific methyltransferase 4B (TRM4B) serves as a potential mRNA m5C methyltransferase. Transcriptome-wide profiling of m5C RNA in Arabidopsis thaliana is made by applying m5C RNA immunoprecipitation followed by a deepsequencing approach (m5C-RIP-seq). LC-MS/MS and dot blot analyses reveal a dynamic pattern of m5C mRNA modification in various tissues and at different developmental stages. m5C-RIP-seq analysis identified 6045m5C peaks in 4465 expressed genes in young seedlings. m5C is enriched in coding sequences with two peaks located immediately after start codons and before stop codons, and is associated with mRNAs with low translation activity. An RNA (cytosine-5)-methyltransferase, tRNA-specific methyltransferase 4B (TRM4B), exhibits m5C RNA methyltransferase activity positively correlated with transcript levels of genes in root development. m5C in mRNA is an epitranscriptome marker in Arabidopsis thaliana, and the regulation of this modification is an integral part of gene regulatory networks underlying plant development
physiological function
enzymes of the cytosine-5 RNA methyltransferase Trm4/NSun2 family methylate tRNAs at C48 and C49 in multiple tRNAs, as well as C34 and C40 in selected tRNAs. Trm4a is responsible for all C48 methylation, which lies in the tRNA variable loop, as well as for C34 in tRNALeuCAA and tRNAProCGG, which are at the anticodon wobble position. Trm4a displays intron-dependent methylation of C34
physiological function
Enzymes of the cytosine-5 RNA methyltransferase Trm4/NSun2 family methylate tRNAs at C48 and C49 in multiple tRNAs, as well as C34 and C40 in selected tRNAs. Trm4b methylates C49 and C50, which both lie in the TPsiC-stem. Trm4b activity of methylation of C34 is independent of the intron
physiological function
the m5C-48/49/50 modifications installed by NSUN2 cluster within the variable loop at the junction with the T-stem. A Levitt pair interaction between C48 and G15 in the D-loop is critical for formation of the characteristic L-shaped tertiary fold of most tRNAs. NSUN2-mediated methylations within the variable loop have also been shown to protect tRNAs against stress-induced, angiogenin-mediated endonucleolytic cleavage. During the maturation of the cytoplasmic tRNALeu(CAA), an m5C34 modification is installed by NSUN2 (cf. EC 2.1.1.203). Cytoplasmic transfer RNAs are methylated by NSUN2, NSUN6, and DNMT2
physiological function
the mRNA of the coiled-coil domain containing 9B (CCDC9B) gene requires NSUN7-mediated methylation for transcript stability. Liver cancer cells exhibiting NSUN7 epigenetic silencing display sensitivity to bromodomain inhibitors
physiological function
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cytoplasmic transfer RNAs are methylated by NSUN2, NSUN6, and DNMT2. Structural differences in PhNSUN6 enable the archaeal enzyme to bind tRNAs containing either U73 or G73, thereby broadening its target spectrum compared to its human homologue enzyme, comparison of NSUN family enzymes, overview. The NSUN family enzymes use the cysteine located in amino acid motif VI for the nucleophilic attack on carbon 6 of the target cytosine in RNA. In all seven human NSUN variants, the catalytic cysteine is preceded by threonine. Hydrogen bonding with the backbone carbonyl of proline and the aspartate side chain in motif IV orients the base in the active site and assists bond formation by transient protonation of the endocyclic N3 of cytidine. The activated nucleobase then accepts a methyl group from the properly positioned SAM cofactor, resulting in the formation of a carbon-carbon bond and generation of S-adenosylhomocysteine (SAH). To complete the reaction, the covalently bound methylated RNA has to be released from the protein. This elimination is assisted by the cysteine located in motif IV of NSUN proteins. This cysteine is located next to the conserved proline and acts as a base to deprotonate the tetrahedral carbon and initiate the elimination reaction that restores the unsaturated m5C heterocycle. m5C72 is reported to promote the thermal stability of PhtRNAs. Roles of m5C RNA methyltransferases in development and disease, overview
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physiological function
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enzymes of the cytosine-5 RNA methyltransferase Trm4/NSun2 family methylate tRNAs at C48 and C49 in multiple tRNAs, as well as C34 and C40 in selected tRNAs. Trm4a is responsible for all C48 methylation, which lies in the tRNA variable loop, as well as for C34 in tRNALeuCAA and tRNAProCGG, which are at the anticodon wobble position. Trm4a displays intron-dependent methylation of C34
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physiological function
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Enzymes of the cytosine-5 RNA methyltransferase Trm4/NSun2 family methylate tRNAs at C48 and C49 in multiple tRNAs, as well as C34 and C40 in selected tRNAs. Trm4b methylates C49 and C50, which both lie in the TPsiC-stem. Trm4b activity of methylation of C34 is independent of the intron
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physiological function
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enzymes of the cytosine-5 RNA methyltransferase Trm4/NSun2 family methylate tRNAs at C48 and C49 in multiple tRNAs, as well as C34 and C40 in selected tRNAs. Trm4a is responsible for all C48 methylation, which lies in the tRNA variable loop, as well as for C34 in tRNALeuCAA and tRNAProCGG, which are at the anticodon wobble position. Trm4a displays intron-dependent methylation of C34
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physiological function
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Enzymes of the cytosine-5 RNA methyltransferase Trm4/NSun2 family methylate tRNAs at C48 and C49 in multiple tRNAs, as well as C34 and C40 in selected tRNAs. Trm4b methylates C49 and C50, which both lie in the TPsiC-stem. Trm4b activity of methylation of C34 is independent of the intron
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physiological function
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cytoplasmic transfer RNAs are methylated by NSUN2, NSUN6, and DNMT2. Structural differences in PhNSUN6 enable the archaeal enzyme to bind tRNAs containing either U73 or G73, thereby broadening its target spectrum compared to its human homologue enzyme, comparison of NSUN family enzymes, overview. The NSUN family enzymes use the cysteine located in amino acid motif VI for the nucleophilic attack on carbon 6 of the target cytosine in RNA. In all seven human NSUN variants, the catalytic cysteine is preceded by threonine. Hydrogen bonding with the backbone carbonyl of proline and the aspartate side chain in motif IV orients the base in the active site and assists bond formation by transient protonation of the endocyclic N3 of cytidine. The activated nucleobase then accepts a methyl group from the properly positioned SAM cofactor, resulting in the formation of a carbon-carbon bond and generation of S-adenosylhomocysteine (SAH). To complete the reaction, the covalently bound methylated RNA has to be released from the protein. This elimination is assisted by the cysteine located in motif IV of NSUN proteins. This cysteine is located next to the conserved proline and acts as a base to deprotonate the tetrahedral carbon and initiate the elimination reaction that restores the unsaturated m5C heterocycle. m5C72 is reported to promote the thermal stability of PhtRNAs. Roles of m5C RNA methyltransferases in development and disease, overview
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physiological function
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cytoplasmic transfer RNAs are methylated by NSUN2, NSUN6, and DNMT2. Structural differences in PhNSUN6 enable the archaeal enzyme to bind tRNAs containing either U73 or G73, thereby broadening its target spectrum compared to its human homologue enzyme, comparison of NSUN family enzymes, overview. The NSUN family enzymes use the cysteine located in amino acid motif VI for the nucleophilic attack on carbon 6 of the target cytosine in RNA. In all seven human NSUN variants, the catalytic cysteine is preceded by threonine. Hydrogen bonding with the backbone carbonyl of proline and the aspartate side chain in motif IV orients the base in the active site and assists bond formation by transient protonation of the endocyclic N3 of cytidine. The activated nucleobase then accepts a methyl group from the properly positioned SAM cofactor, resulting in the formation of a carbon-carbon bond and generation of S-adenosylhomocysteine (SAH). To complete the reaction, the covalently bound methylated RNA has to be released from the protein. This elimination is assisted by the cysteine located in motif IV of NSUN proteins. This cysteine is located next to the conserved proline and acts as a base to deprotonate the tetrahedral carbon and initiate the elimination reaction that restores the unsaturated m5C heterocycle. m5C72 is reported to promote the thermal stability of PhtRNAs. Roles of m5C RNA methyltransferases in development and disease, overview
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physiological function
-
cytoplasmic transfer RNAs are methylated by NSUN2, NSUN6, and DNMT2. Structural differences in PhNSUN6 enable the archaeal enzyme to bind tRNAs containing either U73 or G73, thereby broadening its target spectrum compared to its human homologue enzyme, comparison of NSUN family enzymes, overview. The NSUN family enzymes use the cysteine located in amino acid motif VI for the nucleophilic attack on carbon 6 of the target cytosine in RNA. In all seven human NSUN variants, the catalytic cysteine is preceded by threonine. Hydrogen bonding with the backbone carbonyl of proline and the aspartate side chain in motif IV orients the base in the active site and assists bond formation by transient protonation of the endocyclic N3 of cytidine. The activated nucleobase then accepts a methyl group from the properly positioned SAM cofactor, resulting in the formation of a carbon-carbon bond and generation of S-adenosylhomocysteine (SAH). To complete the reaction, the covalently bound methylated RNA has to be released from the protein. This elimination is assisted by the cysteine located in motif IV of NSUN proteins. This cysteine is located next to the conserved proline and acts as a base to deprotonate the tetrahedral carbon and initiate the elimination reaction that restores the unsaturated m5C heterocycle. m5C72 is reported to promote the thermal stability of PhtRNAs. Roles of m5C RNA methyltransferases in development and disease, overview
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physiological function
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cytoplasmic transfer RNAs are methylated by NSUN2, NSUN6, and DNMT2. Structural differences in PhNSUN6 enable the archaeal enzyme to bind tRNAs containing either U73 or G73, thereby broadening its target spectrum compared to its human homologue enzyme, comparison of NSUN family enzymes, overview. The NSUN family enzymes use the cysteine located in amino acid motif VI for the nucleophilic attack on carbon 6 of the target cytosine in RNA. In all seven human NSUN variants, the catalytic cysteine is preceded by threonine. Hydrogen bonding with the backbone carbonyl of proline and the aspartate side chain in motif IV orients the base in the active site and assists bond formation by transient protonation of the endocyclic N3 of cytidine. The activated nucleobase then accepts a methyl group from the properly positioned SAM cofactor, resulting in the formation of a carbon-carbon bond and generation of S-adenosylhomocysteine (SAH). To complete the reaction, the covalently bound methylated RNA has to be released from the protein. This elimination is assisted by the cysteine located in motif IV of NSUN proteins. This cysteine is located next to the conserved proline and acts as a base to deprotonate the tetrahedral carbon and initiate the elimination reaction that restores the unsaturated m5C heterocycle. m5C72 is reported to promote the thermal stability of PhtRNAs. Roles of m5C RNA methyltransferases in development and disease, overview
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additional information
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four active-site residues critical for Trm4p-mediated tRNA methylation are also required for the formation of the denaturant-resistant complexes with m5C-containing RNA
additional information
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tRNAHis m5C levels are unusually responsive to yeast growth conditions
additional information
catalytic mechanism of the enzyme, comparison of NSUN family enzymes, overview. The NSUN family enzymes use the cysteine located in amino acid motif VI for the nucleophilic attack on carbon 6 of the target cytosine in RNA. In all seven human NSUN variants, the catalytic cysteine is preceded by threonine. Hydrogen bonding with the backbone carbonyl of proline and the aspartate side chain in motif IV orients the base in the active site and assists bond formation by transient protonation of the endocyclic N3 of cytidine. The activated nucleobase then accepts a methyl group from the properly positioned SAM cofactor, resulting in the formation of a carbon-carbon bond and generation of S-adenosylhomocysteine (SAH). To complete the reaction, the covalently bound methylated RNA has to be released from the protein. This elimination is assisted by the cysteine located in motif IV of NSUN proteins. This cysteine is located next to the conserved proline and acts as a base to deprotonate the tetrahedral carbon and initiate the elimination reaction that restores the unsaturated m5C heterocycle
additional information
catalytic mechanism of the enzyme, comparison of NSUN family enzymes, overview. The NSUN family enzymes use the cysteine located in amino acid motif VI for the nucleophilic attack on carbon 6 of the target cytosine in RNA. In all seven human NSUN variants, the catalytic cysteine is preceded by threonine. Hydrogen bonding with the backbone carbonyl of proline and the aspartate side chain in motif IV orients the base in the active site and assists bond formation by transient protonation of the endocyclic N3 of cytidine. The activated nucleobase then accepts a methyl group from the properly positioned SAM cofactor, resulting in the formation of a carbon-carbon bond and generation of S-adenosylhomocysteine (SAH). To complete the reaction, the covalently bound methylated RNA has to be released from the protein. This elimination is assisted by the cysteine located in motif IV of NSUN proteins. This cysteine is located next to the conserved proline and acts as a base to deprotonate the tetrahedral carbon and initiate the elimination reaction that restores the unsaturated m5C heterocycle
additional information
analysis of the catalytic mechanism of the RNA:m5C methyltransferase family, structure-function analysis of RNA:m5C methyltransferases, overview. Lys248, Asp323, Cys326 and Cys373 are the residues at the active site of hNSun6, they are strictly conserved in NSun6s and in the entire RNA:m5CMTase family, suggesting their conserved roles in catalysis. Multiple roles of Lys248 and Asp323. Motif IVCys (C326) plays a role in product release. In the hNSun6/tRNA complex, instead of nucleotide flipping, the acceptor region of tRNA undergoes a complicated conformational reconstitution for access to hNSun6
additional information
-
analysis of the catalytic mechanism of the RNA:m5C methyltransferase family, structure-function analysis of RNA:m5C methyltransferases, overview. Lys248, Asp323, Cys326 and Cys373 are the residues at the active site of hNSun6, they are strictly conserved in NSun6s and in the entire RNA:m5CMTase family, suggesting their conserved roles in catalysis. Multiple roles of Lys248 and Asp323. Motif IVCys (C326) plays a role in product release. In the hNSun6/tRNA complex, instead of nucleotide flipping, the acceptor region of tRNA undergoes a complicated conformational reconstitution for access to hNSun6
additional information
development of m5C-responsive probes, as a strategy for discriminating RNA and DNA m5C methyltransferase activity in cells (cf. EC 2.1.1.37), i.e. the m5C-switchable probe strategy, method development and evaluation, overview. The m5C-probe contains a 5'-terminal fluorescent nucleotide PC (2'-O-methyl 6-phenylpyrrolocytidine), which lights up spontaneously in response to m5C-induced terminal sugar pucker switch. When the probe is unmethylated, pC is able to base-pair with guanine in the complementary strand and stack strongly with its adjacent base. This results in efficient quenching of pC fluorescence through photoinduced electron transfer. m5C methylation of the probe by RNA:m5C MTase (e.g. NSUN2), however, is expected to trigger a C2'-endo to C3'-endo sugar pucker switch in PC and, since the sugar ring pucker defines the glycosidic bond angle, such a change in sugar puckering will also convert the orientation of PC base from axial to equatorial. This, in turn, disrupts its base-pairing and base-stacking interactions, leading to fluorescence activation. Schematic representation of 2'-OMe RNA probes and their methylated counterparts. The composition of the probes is confirmed through MALDI-TOF mass spectrometric analysis
additional information
-
tRNAHis m5C levels are unusually responsive to yeast growth conditions
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NCL1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
684
0
77879
Swiss-Prot
Secretory Pathway (Reliability: 1)
TRM4B_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
685
0
77822
Swiss-Prot
other Location (Reliability: 2)
TRDMT_HUMAN
391
0
44597
Swiss-Prot
other Location (Reliability: 1)
TRDMT_MOUSE
415
0
46794
Swiss-Prot
Mitochondrion (Reliability: 1)
NSUN6_PYRHO
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
389
0
44284
Swiss-Prot
-
NSUN2_HUMAN
767
0
86471
Swiss-Prot
Mitochondrion (Reliability: 3)
NSUN7_HUMAN
718
0
81039
Swiss-Prot
other Location (Reliability: 3)
TRM4A_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
688
0
78515
Swiss-Prot
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80200
x * 80200, calculated from sequence, including Hi26- and thrombin cleavage sequences
82200
x * 82200, SDS-PAGE, recombinant enzyme including Hi26- and thrombin cleavage sequences
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 80200, calculated from sequence, including Hi26- and thrombin cleavage sequences
?
x * 82200, SDS-PAGE, recombinant enzyme including Hi26- and thrombin cleavage sequences
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of NSUN6 with target RNA showing the arrangement and key contacts between the amino acids in the active site and the target cytosine (C72) in RNA (PDB ID 5WWS)
purified recombinant His6-tagged enzyme, hanging drop vapor diffusion method, mixing of 0.001 ml of 4.8 mg/ml protein in 20 mM Tris-HCl, pH 7.0, 300 mM NaCl, 5 mM MgCl2, and 5 mM DTT, with 0.001 ml of reservoir solution consisting of 2% dioxane, 0.1 M bicine, pH 8.6, 18% w/v PEG 8000, and 10 mM yttrium(III) chloride hexahydrate, 16°C. For the hNSun6/tRNA complex, solutions are prepared with 0.075 mM MhNSun6 and 0.075 mM MtRNA, for the hNSun6/tRNA/SAM and hNSun6/tRNA/SFG complexes, hNSun6 is mixed with tRNA at a 1:1 molar ratio, adding either 1 mM SAM or SFG, crystals are obtained by mixing 0.001 ml of this solution with 0.001 ml of reservoir solution containing 0.1 M SPG, pH 8.0-10.0, 24-28% w/v PEG 1500, and 50 mM NaF, X-ray diffraction structure determination and analysis. Of different human tRNACys and tRNAThr isoacceptors and their variants, only tRNACys(GCA)-G2A:C71U can be cocrystallized with hNSun6, molecular replacement using the MTase domain structure of Pyrococcus horikoshii PH0851 (PDB ID: 2YXL) and the PUA domain structure of Pyrococcus horikoshii archaeosine tRNA-guanine transglycosylase (PDB ID: 1J2B) as starting models
Trm4 free and in complex with sinefungin, hanging-drop vapor diffusion, 0.001 ml of protein solution containing 10.8 mg/ml protein with 0.001 ml of crystallization solution containing 100 mM Tris-HCl, pH 7.4, 200 mM MgCl2, 25% PEG 3350, and 6% v/v isopropanol for MJ0026 alone, and 20 100 mM Tris-HCl, pH 7.4, 200 mM MgCl2, 25% PEG 3350, 3 mM sinefungin, and 10 mM cytidine for Mj0026 with sinefungin, cryoprotectant 20% glycerol and 20% PEG 400, respectively, X-ray diffraction structure determination and analysis at 1.27 A and 2.3 A resolutions, respectively
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C271A
-
site-directed mutagenesis, the mutant enzyme forms an irreversible covalent crosslink between itself and the methylated cytosine in its target RNA
C326A
site-directed mutagenesis, tRNA binding structure compared to wild-type enzyme, the C326A mutation hampers the breakdown of the covalent intermediates
D266A
site-directed mutagenesis, the mutant shows highly increased binding affinity for SAM and highly reduced methylation activity
D293A
site-directed mutagenesis, the mutation leads to a loss of SAM binding capability and a loss of methylation activity to tRNACys
D323A
site-directed mutagenesis, the mutant shows highly increased binding affinity for SAM and highly reduced methylation activity
F141A
site-directed mutagenesis, the mutant shows activity similar to wild-type enzyme
G679R
K159A
site-directed mutagenesis, the mutant shows moderately decreased activity compared to wild-type enzyme
K159A/R181A
site-directed mutagenesis, the mutant shows highly decreased activity compared to wild-type enzyme
K160A
site-directed mutagenesis, the mutant shows moderately decreased activity compared to wild-type enzyme
K160A/R181A
site-directed mutagenesis, the mutant shows highly decreased activity compared to wild-type enzyme
K248A
site-directed mutagenesis, the mutant shows 5fold increased binding affinity for SAM
K271A
site-directed mutagenesis, the mutant shows highly increased binding affinity for SAM and highly reduced methylation activity
R181A
site-directed mutagenesis, the mutant shows highly decreased activity compared to wild-type enzyme
C260A
-
the mutant enzyme forms stable RNA-protein complexes in vitro. The complexes are formed due to faulty product release by the modified Trm4p enzyme and contain only natural ribonucleotides within the RNA
C260S
-
the mutant enzyme forms stable RNA-protein complexes in vitro. The complexes are formed due to faulty product release by the modified Trm4p enzyme and contain only natural ribonucleotides within the RNA
C310A
-
the mutant shows only a slightly lower affinity for RNA compared to wild-type Trm4p. The C310A mutant of Trm4p is unable to bind RNA covalently as well as to transfer the methyl group from SAM to the RNA substrate since no activity was detectable
additional information
additional information
-
generation of Arabidopsis thaliana T-DNA insertion mutants of potential mRNA m5C methyltransferases (RCMTs), and of single mutants of TRM4B, trm4b-3 and trm4b-4, the latter exhibit defects in root development. The fulllength transcript of TRM4B and its 3' fragment downstream of the T-DNA insertion sites are greatly decreased in trm4b-3 and undetectable in trm4b-4, implying that trm4b-3 and trm4b-4 could be reduction-of function and loss-of-function mutants, respectively
additional information
-
the only mRNA identified by miCLIP that is differentially expressed when NSun2 is inhibited by RNAi in HEK293 cells is NSun2 itself
additional information
generation of NSUN2 knockout mice (homozygous Nsun2Gt[D014D11]Wrs)
additional information
generation of trm4a and trm4a/trm4b deletion mutants, tRNA methylome of wild-type, trm4aDELTA, trm4bDELTA, and trm4aDELTA/trm4bDELTA as determined by genome-wide high-throughput bisulfite sequencing, overview
additional information
generation of trm4a and trm4a/trm4b deletion mutants, tRNA methylome of wild-type, trm4aDELTA, trm4bDELTA, and trm4aDELTA/trm4bDELTA as determined by genome-wide high-throughput bisulfite sequencing, overview
additional information
generation of trm4b and trm4a/trm4b deletion mutants, tRNA methylome of wild-type, trm4aDELTA, trm4bDELTA, and trm4aDELTA/trm4bDELTA as determined by genome-wide high-throughput bisulfite sequencing, overview
additional information
generation of trm4b and trm4a/trm4b deletion mutants, tRNA methylome of wild-type, trm4aDELTA, trm4bDELTA, and trm4aDELTA/trm4bDELTA as determined by genome-wide high-throughput bisulfite sequencing, overview
additional information
-
generation of trm4a and trm4a/trm4b deletion mutants, tRNA methylome of wild-type, trm4aDELTA, trm4bDELTA, and trm4aDELTA/trm4bDELTA as determined by genome-wide high-throughput bisulfite sequencing, overview
-
additional information
-
generation of trm4b and trm4a/trm4b deletion mutants, tRNA methylome of wild-type, trm4aDELTA, trm4bDELTA, and trm4aDELTA/trm4bDELTA as determined by genome-wide high-throughput bisulfite sequencing, overview
-
additional information
-
generation of trm4a and trm4a/trm4b deletion mutants, tRNA methylome of wild-type, trm4aDELTA, trm4bDELTA, and trm4aDELTA/trm4bDELTA as determined by genome-wide high-throughput bisulfite sequencing, overview
-
additional information
-
generation of trm4b and trm4a/trm4b deletion mutants, tRNA methylome of wild-type, trm4aDELTA, trm4bDELTA, and trm4aDELTA/trm4bDELTA as determined by genome-wide high-throughput bisulfite sequencing, overview
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme HNSun6, hNSun6 and hNSun6-C326A-RNA complexes by nickel affinity chromatography
recombinant MJ0026 from Escherichia coli strain BL21-CodonPlus(DE3)-RIL by heat treatment, anion exchange and hydroxyapatite chromatography, and dialysis
-
recombinant Ybl024p is purified to apparent homogeneity by one-step affinity chromatography on Ni21-NTA-agarose column
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene MJ0026, expression in Escherichia coli strain BL21-CodonPlus(DE3)-RIL
-
inserted in the expression vector pET28b, and the corresponding protein is hyperexpressed in Escherichia coli BL21(DE3)
recombinant expression of His6-tagged wild-type enzyme HNSun6 and mutant enzymes
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
exposure to oxidative stress efficiently repressed NSUN2, causing a reduction of methylation at specific tRNA sites. Nucleophosmin (NPMI) is a marker for nucleolar stress, and a rapid, strong down-regulation of both NPMI and NSUN2 is observed upon arsenite treatment. Additional NSUN family members residing in the mitochondria (NSUN3, NSUN4) and cytoplasm (NSUN6) are similarly repressed in response to arsenite stress
levels of tRNAHis m5C increase following several nutrient starvation treatments of the BY4741 strain, Trm4 protein levels do not increase during starvation conditions
sequenced cDNA libraries prepared from small RNA isolated from NSUN2+/- and NSUN2-/- human fibroblasts reveal that eight of the 43 ncRNAs are differentially regulated
-
exposure to oxidative stress efficiently repressed NSUN2, causing a reduction of methylation at specific tRNA sites. Nucleophosmin (NPMI) is a marker for nucleolar stress, and a rapid, strong down-regulation of both NPMI and NSUN2 is observed upon arsenite treatment. Additional NSUN family members residing in the mitochondria (NSUN3, NSUN4) and cytoplasm (NSUN6) are similarly repressed in response to arsenite stress
exposure to oxidative stress efficiently repressed NSUN2, causing a reduction of methylation at specific tRNA sites. Nucleophosmin (NPMI) is a marker for nucleolar stress, and a rapid, strong down-regulation of both NPMI and NSUN2 is observed upon arsenite treatment. Additional NSUN family members residing in the mitochondria (NSUN3, NSUN4) and cytoplasm (NSUN6) are similarly repressed in response to arsenite stress
levels of tRNAHis m5C increase following several nutrient starvation treatments of the BY4741 strain, Trm4 protein levels do not increase during starvation conditions
-
levels of tRNAHis m5C increase following several nutrient starvation treatments of the BY4741 strain, Trm4 protein levels do not increase during starvation conditions
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
NSUN7 epigenetic inactivation by promoter CpG island hypermethylation is common in liver malignant cells. DNA methylation-associated loss of NSUN7 is also observed in primary liver tumors where it is associated with poor overall survival. Liver cancer cells exhibiting NSUN7 epigenetic silencing display sensitivity to bromodomain inhibitors
molecular biology
a CRISPR-Cas13d-based tool, named reengineered m5C modification system (RCMS), for targeted m5C methylation and demethylation in specific transcripts. A nuclear-localized dCasRx conjugated to either a methyltransferase, NSUN2/NSUN6, or a demethylase, the catalytic domain of mouse Tet2 (ten-eleven translocation 2), enables the manipulation of methylation events at precise m5C sites. It is effective in modulating m5C levels within transfer RNAs
additional information
additional information
changes in tRNA methylation profiles are sufficient to specify cellular metabolic states and efficiently adapt protein synthesis rates to cell stress
additional information
changes in tRNA methylation profiles are sufficient to specify cellular metabolic states and efficiently adapt protein synthesis rates to cell stress
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Motorin, Y.; Grosjean, H.
Multisite-specific tRNA:m5C-methyltransferase (Trm4) in yeast Saccharomyces cerevisiae: identification of the gene and substrate specificity of the enzyme
RNA
5
1105-1118
1999
Saccharomyces cerevisiae (P38205), Saccharomyces cerevisiae
brenda
King, M.Y.; Redman, K.L.
RNA methyltransferases utilize two cysteine residues in the formation of 5-methylcytosine
Biochemistry
41
11218-11225
2002
Saccharomyces cerevisiae
brenda
Redman, K.L.
Assembly of protein-RNA complexes using natural RNA and mutant forms of an RNA cytosine methyltransferase
Biomacromolecules
7
3321-3326
2006
Saccharomyces cerevisiae
brenda
Strobel, M.C.; Abelson, J.
Effect of intron mutations on processing and function of Saccharomyces cerevisiae SUP53 tRNA in vitro and in vivo
Mol. Cell. Biol.
6
2663-2673
1986
Saccharomyces cerevisiae
brenda
Jiang, H.Q.; Motorin, Y.; Jin, Y.X.; Grosjean, H.
Pleiotropic effects of intron removal on base modification pattern of yeast tRNAPhe: an in vitro study
Nucleic Acids Res.
25
2694-2701
1997
Saccharomyces cerevisiae, Saccharomyces cerevisiae Pp1001
brenda
Brzezicha, B.; Schmidt, M.; Makalowska, I.; Jarmolowski, A.; Pienkowska, J.; Szweykowska-Kulinska, Z.
Identification of human tRNA:m5C methyltransferase catalysing intron-dependent m5C formation in the first position of the anticodon of the pre-tRNA Leu(CAA)
Nucleic Acids Res.
34
6034-6043
2006
Saccharomyces cerevisiae (P38205), Saccharomyces cerevisiae
brenda
Walbott, H.; Husson, C.; Auxilien, S.; Golinelli-Pimpaneau, B.
Cysteine of sequence motif VI is essential for nucleophilic catalysis by yeast tRNA m5C methyltransferase
RNA
13
967-973
2007
Saccharomyces cerevisiae
brenda
Awai, T.; Ochi, A.; Ihsanawati, A.; Sengoku, T.; Hirata, A.; Bessho, Y.; Yokoyama, S.; Hori, H.
Substrate tRNA recognition mechanism of a multisite-specific tRNA methyltransferase, Aquifex aeolicus Trm1, based on the X-ray crystal structure
J. Biol. Chem.
286
35236-35246
2011
Methanocaldococcus jannaschii
brenda
Moon, H.J.; Redman, K.L.
Trm4 and Nsun2 RNA:m5C methyltransferases form metabolite-dependent, covalent adducts with previously methylated RNA
Biochemistry
53
7132-7144
2014
Saccharomyces cerevisiae
brenda
Burgess, A.; David, R.; Searle, I.
Conservation of tRNA and rRNA 5-methylcytosine in the kingdom Plantae
BMC Plant Biol.
15
199
2015
Arabidopsis thaliana, Brassica rapa, Caulerpa taxifolia, Ginkgo biloba, Nannochloropsis oculata, Triticum turgidum subsp. durum
brenda
Hussain, S.; Sajini, A.A.; Blanco, S.; Dietmann, S.; Lombard, P.; Sugimoto, Y.; Paramor, M.; Gleeson, J.G.; Odom, D.T.; Ule, J.; Frye, M.
NSun2-mediated cytosine-5 methylation of vault noncoding RNA determines its processing into regulatory small RNAs
Cell Rep.
4
255-261
2013
Homo sapiens
brenda
Khoddami, V.; Cairns, B.R.
Identification of direct targets and modified bases of RNA cytosine methyltransferases
Nat. Biotechnol.
31
458-464
2013
Homo sapiens
brenda
Preston, M.; DSilva, S.; Kon, Y.; Phizicky, E.
TRNAHis 5-methylcytidine levels increase in response to several growth arrest conditions in Saccharomyces cerevisiae
RNA
19
243-256
2013
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Bohnsack, K.; Hoebartner, C.; Bohnsack, M.
Eukaryotic 5-methylcytosine (M5C) RNA methyltransferases mechanisms, cellular functions, and links to disease
Genes (Basel)
10
102
2019
Homo sapiens (Q08J23), Homo sapiens (Q8TEA1), Pyrococcus horikoshii (O57712), Pyrococcus horikoshii ATCC 700860 (O57712), Pyrococcus horikoshii DSM 12428 (O57712), Pyrococcus horikoshii JCM 9974 (O57712), Pyrococcus horikoshii NBRC 100139 (O57712), Pyrococcus horikoshii OT-3 (O57712)
brenda
Cui, X.; Liang, Z.; Shen, L.; Zhang, Q.; Bao, S.; Geng, Y.; Zhang, B.; Leo, V.; Vardy, L.A.; Lu, T.; Gu, X.; Yu, H.
5-Methylcytosine RNA methylation in Arabidopsis thaliana
Mol. Plant
10
1387-1399
2017
Arabidopsis thaliana
brenda
Liu, R.; Long, T.; Li, J.; Li, H.; Wang, E.
Structural basis for substrate binding and catalytic mechanism of a human RNA m5C methyltransferase NSun6
Nucleic Acids Res.
45
6684-6697
2017
Homo sapiens (Q8TEA1), Homo sapiens, Schizosaccharomyces pombe (Q9HGQ2), Schizosaccharomyces pombe (O13935), Schizosaccharomyces pombe 972 (Q9HGQ2), Schizosaccharomyces pombe 972 (O13935), Schizosaccharomyces pombe ATCC 24843 (Q9HGQ2), Schizosaccharomyces pombe ATCC 24843 (O13935)
brenda
Yang, T.; Low, J.J.A.; Woon, E.C.Y.
A general strategy exploiting m5C duplex-remodelling effect for selective detection of RNA and DNA m5C methyltransferase activity in cells
Nucleic Acids Res.
48
e5
2020
Homo sapiens (O14717)
brenda
Gkatza, N.A.; Castro, C.; Harvey, R.F.; Heiss, M.; Popis, M.C.; Blanco, S.; Borneloev, S.; Sajini, A.A.; Gleeson, J.G.; Griffin, J.L.; West, J.A.; Kellner, S.; Willis, A.E.; Dietmann, S.; Frye, M.
Cytosine-5 RNA methylation links protein synthesis to cell metabolism
PLoS Biol.
17
e3000297
2019
Mus musculus (O55055), Homo sapiens (O14717)
brenda
Flores, J.V.; Cordero-Espinoza, L.; Oeztuerk-Winder, F.; Andersson-Rolf, A.; Selmi, T.; Blanco, S.; Tailor, J.; Dietmann, S.; Frye, M.
Cytosine-5 RNA methylation regulates neural stem cell differentiation and motility
Stem Cell Reports
8
112-124
2017
Homo sapiens (O14717), Mus musculus (O55055)
brenda
Ortiz-Barahona, V.; Soler, M.; Davalos, V.; Garcia-Prieto, C.A.; Janin, M.; Setien, F.; Fernandez-Rebollo, I.; Bech-Serra, J.J.; De La Torre, C.; Guil, S.; Villanueva, A.; Zhang, P.H.; Yang, L.; Guarnacci, M.; Schumann, U.; Preiss, T.; Balaseviciute, U.; Montal, R.; Llovet, J.M.; Esteller, M.
Epigenetic inactivation of the 5-methylcytosine RNA methyltransferase NSUN7 is associated with clinical outcome and therapeutic vulnerability in liver cancer
Mol. Cancer
22
83
2023
Homo sapiens (Q8NE18)
brenda
Zhang, T.; Zhao, F.; Li, J.; Sun, X.; Zhang, X.; Wang, H.; Fan, P.; Lai, L.; Li, Z.; Sui, T.
Programmable RNA 5-methylcytosine (m5C) modification of cellular RNAs by dCasRx conjugated methyltransferase and demethylase
Nucleic Acids Res.
52
2776-2791
2024
Homo sapiens (Q8TEA1)
brenda
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