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Information on EC 2.1.1.200 - tRNA (cytidine32/uridine32-2'-O)-methyltransferase
for references in articles please use BRENDA:EC2.1.1.200
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.200 tRNA (cytidine32/uridine32-2'-O)-methyltransferase
IUBMB Comments
In Escherichia coli YfhQ is the only methyltransferase responsible for the formation of 2′-O-methylcytidine32 in tRNA. No methylation of cytosine34 in tRNALeu(CAA). In vitro the enzyme 2-O-methylates cytidine32 of tRNASer1 and uridine32 of tRNAGln2.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
show+
cytidine32 in tRNA
=
+
2'-O-methylcytidine32 in tRNA
+
uridine32 in tRNA
=
+
2'-O-methyluridine32 in tRNA
Synonyms
trmet(xm32), trna:cm32/um32 methyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PA14 14690
Saci_0621
TrmJ
tRNA (cytidine(32)/uridine(32)/adenosine(32)-2'-O)-methyltransferase
tRNA:Cm32/Um32/Am32 methyltransferase
tRNA (cytidine(32)/uridine(32)/adenosine(32)-2'-O)-methyltransferase
-
tRNA (cytidine(32)/uridine(32)/adenosine(32)-2'-O)-methyltransferase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + cytidine32 in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
-
-
-
-
S-adenosyl-L-methionine + uridine32 in tRNA = S-adenosyl-L-homocysteine + 2'-O-methyluridine32 in tRNA
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (cytidine32/uridine32-2'-O)-methyltransferase
In Escherichia coli YfhQ is the only methyltransferase responsible for the formation of 2'-O-methylcytidine32 in tRNA. No methylation of cytosine34 in tRNALeu(CAA). In vitro the enzyme 2-O-methylates cytidine32 of tRNASer1 and uridine32 of tRNAGln2.
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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 + adenine32 in tRNAPro(GGG)
S-adenosyl-L-homocysteine + 2'-O-methyladenine32 in tRNAPro(GGG)
S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
S-adenosyl-L-methionine + cytidine32 in tRNAMet(CAU)
S-adenosyl-L-homocysteine + 2'-O-methylcytisine32 in tRNA
S-adenosyl-L-methionine + cytidine32 in tRNATrp(CCA)
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNATrp(CCA)
S-adenosyl-L-methionine + nucleoside32 in EctRNAfMet1(CAU)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNAfMet1(CAU)
S-adenosyl-L-methionine + nucleoside32 in EctRNAfMet2(CAU)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNAfMet2(CAU)
S-adenosyl-L-methionine + nucleoside32 in EctRNAGln1(UUG)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNAGln1(UUG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + nucleoside32 in EctRNAGln2(CUG)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNAGln2(CUG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + nucleoside32 in EctRNASer1(UGA)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNASer1(UGA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + nucleoside32 in EctRNATrp1(CCA)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNATrp1(CCA)
S-adenosyl-L-methionine + nucleoside32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in tRNA
S-adenosyl-L-methionine + uridine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine32 in tRNA
S-adenosyl-L-methionine + uridine32 in tRNAGln(UUG)
S-adenosyl-L-homocysteine + 2'-O-methyluridine32 in tRNAGln(UUG)
S-adenosyl-L-methionine + uridine32 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 2'-O-methyluridine32 in tRNAPro(CGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine32 in tRNAPro(UGG)
S-adenosyl-L-homocysteine + 2'-O-methyluridine32 in tRNAPro(UGG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine32 in tRNAPro(GGG)
S-adenosyl-L-homocysteine + 2'-O-methyladenine32 in tRNAPro(GGG)
Substrates: tRNAPro(GGG) is the most efficient substrate, with methyladenine formation an order of magnitude higher than methyluridine or methylcytidine in other substrates
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine32 in tRNAPro(GGG)
S-adenosyl-L-homocysteine + 2'-O-methyladenine32 in tRNAPro(GGG)
Substrates: tRNAPro(GGG) is the most efficient substrate, with methyladenine formation an order of magnitude higher than methyluridine or methylcytidine in other substrates
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
Substrates: presence of 2'-O-methylated cytidine at position 32 in tRNAfMet1(CAU), tRNAfMet2(CAU), tRNASer1(UGA), and tRNATrp1(CCA). In Escherichia coli YfhQ is the only methyltransferase responsible for the formation of Cm32 in tRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
Substrates: 2'-O-methylation of cytidine34 in tRNAGln2(CUG). Total crude tRNA extracted from the wild-type strain MC1061 was not a substrate for the purified YfhQ enzyme, while tRNA from the yfhQ K.O. strain is an excellent substrate for this enzyme
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
Substrates: while the four canonical nucleosides are substrates of the Escherichia coli enzyme at position 32 of tRNA, the archaeal TrmJ can only methylate the ribose of a cytidine
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
Substrates: while the four canonical nucleosides are substrates of the Escherichia coli enzyme at position 32 of tRNA, the archaeal TrmJ can only methylate the ribose of a cytidine
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine32 in tRNAMet(CAU)
S-adenosyl-L-homocysteine + 2'-O-methylcytisine32 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine32 in tRNAMet(CAU)
S-adenosyl-L-homocysteine + 2'-O-methylcytisine32 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine32 in tRNATrp(CCA)
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNATrp(CCA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine32 in tRNATrp(CCA)
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNATrp(CCA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + nucleoside32 in EctRNAfMet1(CAU)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNAfMet1(CAU)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + nucleoside32 in EctRNAfMet1(CAU)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNAfMet1(CAU)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + nucleoside32 in EctRNAfMet2(CAU)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNAfMet2(CAU)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + nucleoside32 in EctRNAfMet2(CAU)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNAfMet2(CAU)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + nucleoside32 in EctRNATrp1(CCA)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNATrp1(CCA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + nucleoside32 in EctRNATrp1(CCA)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNATrp1(CCA)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + nucleoside32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + nucleoside32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine32 in tRNA
Substrates: presence of 2'-O-methylated uridine in position 32 of the anticodon loop in tRNAGln1(UUG) and tRNAGln2(CUG)
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine32 in tRNA
Substrates: 2'-O-methylation of uridine34 tRNASer1(UGA). Total crude tRNA extracted from the wild-type strain MC1061 was not a substrate for the purified YfhQ enzyme, while tRNA from the yfhQ K.O. strain is an excellent substrate for this enzyme
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine32 in tRNAGln(UUG)
S-adenosyl-L-homocysteine + 2'-O-methyluridine32 in tRNAGln(UUG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine32 in tRNAGln(UUG)
S-adenosyl-L-homocysteine + 2'-O-methyluridine32 in tRNAGln(UUG)
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: no methylation of cytosine 34 in tRNALeu(CAA)
Products: -
Products: -
?
additional information
?
-
-
Substrates: no methylation of cytosine 34 in tRNALeu(CAA)
Products: -
Products: -
?
additional information
?
-
Substrates: bacterial TrmJs recognize substrate tRNAs and specifically catalyze a 2'-O modification at ribose 32. All six Escherichia coli tRNAs with 2'-O-methylated nucleosides at position 32 are substrates of EcTrmJ. The elbow region of tRNA, but not the amino acid acceptor stem, is needed for the methylation reaction. tRNA recognition by EcTrmJ involves the cooperative influences of conserved residues from both the SPOUT and extensional domains, and this process is regulated by the flexible hinge region that connects these two domains
Products: -
Products: -
?
additional information
?
-
Substrates: bacterial TrmJs recognize substrate tRNAs and specifically catalyze a 2'-O modification at ribose 32. All six Escherichia coli tRNAs with 2'-O-methylated nucleosides at position 32 are substrates of EcTrmJ. The elbow region of tRNA, but not the amino acid acceptor stem, is needed for the methylation reaction. tRNA recognition by EcTrmJ involves the cooperative influences of conserved residues from both the SPOUT and extensional domains, and this process is regulated by the flexible hinge region that connects these two domains
Products: -
Products: -
?
additional information
?
-
Substrates: PA14 TrmJ catalyzes 2'-O-methylation of C, U and A at position 32 in the tRNA anticodon loop. tRNA substrates for reaction with PA14 TrmJ are prepared by in vitro T7 transcription. Substrate specificity, overview. No or poor activity with tRNASer(UGA) and tRNAHis(GUG). Structure analysis of TrmJ-NTD tRNA binding
Products: -
Products: -
?
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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 + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
S-adenosyl-L-methionine + nucleoside32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in tRNA
S-adenosyl-L-methionine + uridine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine32 in tRNA
Substrates: presence of 2'-O-methylated uridine in position 32 of the anticodon loop in tRNAGln1(UUG) and tRNAGln2(CUG)
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
Substrates: presence of 2'-O-methylated cytidine at position 32 in tRNAfMet1(CAU), tRNAfMet2(CAU), tRNASer1(UGA), and tRNATrp1(CCA). In Escherichia coli YfhQ is the only methyltransferase responsible for the formation of Cm32 in tRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + nucleoside32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + nucleoside32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in tRNA
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: bacterial TrmJs recognize substrate tRNAs and specifically catalyze a 2'-O modification at ribose 32. All six Escherichia coli tRNAs with 2'-O-methylated nucleosides at position 32 are substrates of EcTrmJ. The elbow region of tRNA, but not the amino acid acceptor stem, is needed for the methylation reaction. tRNA recognition by EcTrmJ involves the cooperative influences of conserved residues from both the SPOUT and extensional domains, and this process is regulated by the flexible hinge region that connects these two domains
Products: -
Products: -
?
additional information
?
-
Substrates: bacterial TrmJs recognize substrate tRNAs and specifically catalyze a 2'-O modification at ribose 32. All six Escherichia coli tRNAs with 2'-O-methylated nucleosides at position 32 are substrates of EcTrmJ. The elbow region of tRNA, but not the amino acid acceptor stem, is needed for the methylation reaction. tRNA recognition by EcTrmJ involves the cooperative influences of conserved residues from both the SPOUT and extensional domains, and this process is regulated by the flexible hinge region that connects these two domains
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
sinefungin
SAM analogue, enzyme binding structure analysis from complex crystal structure, structure of TrmJ-NTD bound to sinefungin, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00067
nucleoside32 in EctRNAfMet1(CAU)
pH 9.0, 37°C, recombinant wild-type enzyme
-
0.00081
nucleoside32 in EctRNAfMet2(CAU)
pH 9.0, 37°C, recombinant wild-type enzyme
-
0.00988
nucleoside32 in EctRNAGln1(UUG)
pH 9.0, 37°C, recombinant wild-type enzyme
-
0.00579
nucleoside32 in EctRNAGln2(CUG)
pH 9.0, 37°C, recombinant wild-type enzyme
-
0.01182
nucleoside32 in EctRNASer1(UGA)
pH 9.0, 37°C, recombinant wild-type enzyme
-
0.00094
nucleoside32 in EctRNATrp1(CCA)
pH 9.0, 37°C, recombinant wild-type enzyme
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0253
nucleoside32 in EctRNAfMet1(CAU)
pH 9.0, 37°C, recombinant wild-type enzyme
-
0.0237
nucleoside32 in EctRNAfMet2(CAU)
pH 9.0, 37°C, recombinant wild-type enzyme
-
0.02
nucleoside32 in EctRNAGln1(UUG)
pH 9.0, 37°C, recombinant wild-type enzyme
-
0.0235
nucleoside32 in EctRNAGln2(CUG)
pH 9.0, 37°C, recombinant wild-type enzyme
-
0.0383
nucleoside32 in EctRNASer1(UGA)
pH 9.0, 37°C, recombinant wild-type enzyme
-
0.0218
nucleoside32 in EctRNATrp1(CCA)
pH 9.0, 37°C, recombinant wild-type enzyme
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
TrmJ proteins from the SPOUT methyltransferase superfamily are tRNA Xm32 modification enzymes that occur in bacteria and archaea. Unlike archaeal TrmJ, bacterial TrmJ require full-length tRNA molecules as substrates
evolution
PA14 14690 possesses the conserved region of TrmJ-specific motif, a consensus TXARXR sequence (residues 79-84). This motif has been shown to be critical for binding of SAM/SAH and tRNA. PA14 14690 also contains a conserved Arg at position 23, which is proposed to be involved in its catalytic activity. Another catalytic residue, the Tyr at position 141, is replaced by Phe. In addition to Arg positions 82 and 84 in the TrmJ-specific motif, PA14 14690 also contains more key conserved tRNA binding residues including arginine at positions 100, 101 and 105
evolution
-
TrmJ proteins from the SPOUT methyltransferase superfamily are tRNA Xm32 modification enzymes that occur in bacteria and archaea. Unlike archaeal TrmJ, bacterial TrmJ require full-length tRNA molecules as substrates
-
evolution
-
PA14 14690 possesses the conserved region of TrmJ-specific motif, a consensus TXARXR sequence (residues 79-84). This motif has been shown to be critical for binding of SAM/SAH and tRNA. PA14 14690 also contains a conserved Arg at position 23, which is proposed to be involved in its catalytic activity. Another catalytic residue, the Tyr at position 141, is replaced by Phe. In addition to Arg positions 82 and 84 in the TrmJ-specific motif, PA14 14690 also contains more key conserved tRNA binding residues including arginine at positions 100, 101 and 105
-
malfunction
loss of trmJ causes an increased susceptibility to H2O2. Phenotypic analysis of cytotoxicity induced by H2O2 in PA14 wild-type strain, trmJ mutant strain, and the trmJ complementation strain or trmJC, overview. Inactivation of trmJ abolishes Cm, Um, or Am formation in Pseudomonas aeruginosa tRNA
malfunction
-
loss of trmJ causes an increased susceptibility to H2O2. Phenotypic analysis of cytotoxicity induced by H2O2 in PA14 wild-type strain, trmJ mutant strain, and the trmJ complementation strain or trmJC, overview. Inactivation of trmJ abolishes Cm, Um, or Am formation in Pseudomonas aeruginosa tRNA
-
metabolism
methylation at position 32 of tRNA catalyzed by TrmJ alters oxidative stress response in Pseudomonas aeruginosa
metabolism
-
methylation at position 32 of tRNA catalyzed by TrmJ alters oxidative stress response in Pseudomonas aeruginosa
-
physiological function
methylation of ribose moieties in tRNA is frequent, especially at position 32 where it is commonplace in all three domains of life
physiological function
PA14 trmJ encodes a tRNA (cytidine(32)/uridine(32)/adenosine(32)-2'-O)-methyltransferase that regulates the expression of oxidative stress response genes. Role of tRNA modifications in the oxidative stress response of prokaryotes. TrmJ is a tRNA:Cm32/Um32/Am32 methyltransferase involved in translational fidelity and the oxidative stress response. TrmJ confers H2O2 resistance in part by upregulating the expression of catalase genes
physiological function
-
methylation of ribose moieties in tRNA is frequent, especially at position 32 where it is commonplace in all three domains of life
-
physiological function
-
PA14 trmJ encodes a tRNA (cytidine(32)/uridine(32)/adenosine(32)-2'-O)-methyltransferase that regulates the expression of oxidative stress response genes. Role of tRNA modifications in the oxidative stress response of prokaryotes. TrmJ is a tRNA:Cm32/Um32/Am32 methyltransferase involved in translational fidelity and the oxidative stress response. TrmJ confers H2O2 resistance in part by upregulating the expression of catalase genes
-
additional information
semi-quantitative real-time PCR analysis of oxyR, katA, katB, katE, ankB and recG transcripts in response to H2O2. Analysis of ribonucleosides by HPLC-coupled tandem quadrupole mass spectrometry
additional information
-
semi-quantitative real-time PCR analysis of oxyR, katA, katB, katE, ankB and recG transcripts in response to H2O2. Analysis of ribonucleosides by HPLC-coupled tandem quadrupole mass spectrometry
-
Show AA Sequence and Transmembrane Helices (8015 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
the dimerization of C-terminal domain is important for the catalytic activity of EcTrmJ
additional information
-
the dimerization of C-terminal domain is important for the catalytic activity of EcTrmJ
-
additional information
the free catalytic N-terminal domain of TrmJ shows a 2fold symmetrical dimer with an active site located at the interface between the monomers and a flexible basic loop positioned to bind tRNA, with conformational changes upon binding of the SAM-analogue sinefungin. Analysis of the structure of the N-terminal domain of TrmJ, overview. Residues 166-GKPTKMEK-173 connect the N- to the C-terminal domain of TrmJ in a flexible way in the absence of a tRNA ligand
additional information
-
the free catalytic N-terminal domain of TrmJ shows a 2fold symmetrical dimer with an active site located at the interface between the monomers and a flexible basic loop positioned to bind tRNA, with conformational changes upon binding of the SAM-analogue sinefungin. Analysis of the structure of the N-terminal domain of TrmJ, overview. Residues 166-GKPTKMEK-173 connect the N- to the C-terminal domain of TrmJ in a flexible way in the absence of a tRNA ligand
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant C-terminally His6-tagged wild-type enzyme, hanging drop vapour diffusion method, mixing of 10 mg/ml of protein 20 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM MgCl2, and 2 mM S-adenosyl-L-homocysteine, with 3.6 M NaCl and 0.1 M HEPES, pH 8.2, 20°C, 2 months, X-ray diffraction structure determination and analysis, full-length EcTrmJ forms an unusual dimer in the asymmetric unit, with both the catalytic SPOUT domain and C-terminal extension forming separate dimeric associations in the crystal structure, molecular replacement
recombinant TrmJ-NTD protein, hanging drop vapour diffusion method, mixing of 0.001 ml of 20 mg/ml protein solution with 0.002 ml of reservoir solution containing Bis-Tris propane, pH 6.5, 0.2 M ammonium chloride, 25% w/v PEG 3350, 20°C, or with 0.03 M MgCl2, 0.03 M CaCl2, 20% w/v PEG MME550, 10% w/v PEG 20000, and 0.1 M MOPS/Na-HEPES, pH 7.5, and soaking with 1 mM sinefungin, 20°C, resulting in two different crystal forms, method optimization, X-ray diffraction structure determination and analysis at 1.7 A and 1.8-2.2 A resolution, respectively
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F199A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
I228A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
F199A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
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additional information
additional information
generation of several partial deletion mutants of TrmJ, including single site mutants, DELTA2 (deleted residues 171-172), DELTA4 (deleted residues 171-174), DELTA7 (deleted residues 169-175), DELTA10 (deleted residues 167-176), DELTA12 (deleted residues 166-177), NTD (residues 1-170) and CTD (residues 171-246)
additional information
-
generation of several partial deletion mutants of TrmJ, including single site mutants, DELTA2 (deleted residues 171-172), DELTA4 (deleted residues 171-174), DELTA7 (deleted residues 169-175), DELTA10 (deleted residues 167-176), DELTA12 (deleted residues 166-177), NTD (residues 1-170) and CTD (residues 171-246)
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged wild-type enzyme and deletion mutants from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant His-tagged complete TrmJ protein spanning residues 1-257 (TrmJ) and His-tagged N-terminal SAM-binding domain, residues 1-167, from Escherichia coli strain BL21(DE3) Rosetta T1R by nickel affinity chromatography and two different steps of gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene trmJ, recombinant expression of His-tagged complete TrmJ protein spanning residues 1-257 (TrmJ) and of His-tagged N-terminal SAM-binding domain, residues 1-167, in Escherichia coli strain BL21(DE3) Rosetta T1R, complementation of a trmJ mutant strain by expression of the endogenous full-length enzyme
recombinant expression of C-terminally His6-tagged wild-type enzyme and deletion mutants in Escherichia coli strain BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Purta, E.; van Vliet, F.; Tkaczuk, K.L.; Dunin-Horkawicz, S.; Mori, H.; Droogmans, L.; Bujnicki, J.M.
The yfhQ gene of Escherichia coli encodes a tRNA:Cm32/Um32 methyltransferase
BMC Mol. Biol.
7
23
2006
Escherichia coli (P0AE01), Escherichia coli
brenda
Somme, J.; Van Laer, B.; Roovers, M.; Steyaert, J.; Versees, W.; Droogmans, L.
Characterization of two homologous 2'-O-methyltransferases showing different specificities for their tRNA substrates
RNA
20
1257-1271
2014
Sulfolobus acidocaldarius (Q4JB16), Sulfolobus acidocaldarius DSM 639 (Q4JB16)
brenda
Liu, R.J.; Long, T.; Zhou, M.; Zhou, X.L.; Wang, E.D.
tRNA recognition by a bacterial tRNA Xm32 modification enzyme from the SPOUT methyltransferase superfamily
Nucleic Acids Res.
43
7489-7503
2015
Escherichia coli (P0AE01), Escherichia coli K-12 MG1655 (P0AE01)
brenda
Jaroensuk, J.; Atichartpongkul, S.; Chionh, Y.; Hwa Wong, Y.; Liew, C.; McBee, M.; Thongdee, N.; Prestwich, E.; DeMott, M.; Mongkolsuk, S.; Dedon, P.; Lescar, J.; Fuangthong, M.
Methylation at position 32 of tRNA catalyzed by TrmJ alters oxidative stress response in Pseudomonas aeruginosa
Nucleic Acids Res.
44
10834-10848
2016
Pseudomonas aeruginosa (A0A0H2ZF87), Pseudomonas aeruginosa UCBPP-PA14 (A0A0H2ZF87)
brenda
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