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Information on EC 2.1.1.216 - tRNA (guanine26-N2)-dimethyltransferase
for references in articles please use BRENDA:EC2.1.1.216
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.216 tRNA (guanine26-N2)-dimethyltransferase
IUBMB Comments
The enzyme dissociates from its tRNA substrate between the two consecutive methylation reactions. In contrast to EC 2.1.1.215, tRNA (guanine26-N2/guanine27-N2)-dimethyltransferase, this enzyme does not catalyse the methylation of guanine27 in tRNA.
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Reaction Schemes
show2
+
guanine26 in tRNA
=
2
+
N2-dimethylguanine26 in tRNA
Synonyms
trm1p, zc376.5, ta0997, trna (m22g26)dimethyltransferase, trm1 methyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 2.1.1.32
-
-
formerly, part transferred
-
Ta0997
transfer RNA methyltransferase
Trm1
Trm1p
tRNA(m22G26)dimethyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 S-adenosyl-L-methionine + guanine26 in tRNA = 2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 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 (guanine26-N2)-dimethyltransferase
The enzyme dissociates from its tRNA substrate between the two consecutive methylation reactions. In contrast to EC 2.1.1.215, tRNA (guanine26-N2/guanine27-N2)-dimethyltransferase, this enzyme does not catalyse the methylation of guanine27 in tRNA.
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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
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNA
2 S-adenosyl-L-methionine + guanine26 in tRNALeu(UAG)
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeu(UAG)
2 S-adenosyl-L-methionine + guanine26 in tRNAPhe
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNAPhe
2 S-adenosyl-L-methionine + guanine26 in tRNASer
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNASer
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNATyr
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNATyr
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 2'-O-methylguanine26 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-dimethylguanine26 in elongator tRNAMet
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 2'-O-methylguanine26 in initiator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-dimethylguanine26 in initiator tRNAMet
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylguanine26 in elongator tRNAMet
S-adenosyl-L-methionine + guanine26 in initiator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylguanine26 in initiator tRNAMet
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
S-adenosyl-L-methionine + guanine26 in tRNAPhe
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNAPhe
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
S-adenosyl-L-methionine + N2-methylguanine26 in tRNAPhe
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNAPhe
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNA
Substrates: wild-type enzyme produces 88% N2-dimethylguanine26 tRNA and 12% N2-methylguanine26 in tRNA. The Caenorhabditis elegans tRNA(m22G26)dimethyltransferase efficiently recognized the Escherichia coli tRNA as a substrate in vivo, and that the enzyme is capable of both mono- and dimethylating G26 in this tRNA
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNA
-
Substrates: the efficient dimethylation of guanine26 requires the presence of base-pairs C11*G24 and G10*C25 and a variable loop of five bases within a correct 3D-core of the tRNA molecule. These identity elements probably ensure the correct presentation of methylated m2G26 to the enzyme for the attachment of the second methyl group
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNA
-
Substrates: the efficient dimethylation of guanine26 requires the presence of base-pairs C11*G24 and G10*C25 and a variable loop of five bases within a correct 3D-core of the tRNA molecule. These identity elements probably ensure the correct presentation of methylated m2G26 to the enzyme for the attachment of the second methyl group. The methylated intermediate, and the enzyme dissociates from its tRNA substrate between the two consecutive methylation reactions
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNA
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNA
Substrates: wild-type enzyme produces 94% N2-dimethylguanine26 tRNA and 6% N2-methylguanine26 in tRNA
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNA
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNA
-
Substrates: the elements necessary for a productive interaction between G26 in nuclear coded yeast tRNAs and the yeast G26 modifying enzyme are located within the core of the tRNA
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNALeu(UAG)
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeu(UAG)
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNALeu(UAG)
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeu(UAG)
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNALeu(UAG)
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeu(UAG)
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNALeu(UAG)
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeu(UAG)
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNALeu(UAG)
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeu(UAG)
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNAPhe
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNAPhe
-
Substrates: tRNAPhe from yeast, the efficient dimethylation of guanine26 requires the presence of base-pairs C11*G24 and G10*C25 and a variable loop of five bases within a correct 3D-core of the tRNA molecule. These identity elements probably ensure the correct presentation of methylated m2G26 to the enzyme for the attachment of the second methyl group
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNAPhe
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNAPhe
Substrates: tRNAPhe from yeast
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylguanine26 in elongator tRNAMet
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylguanine26 in elongator tRNAMet
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylguanine26 in elongator tRNAMet
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylguanine26 in elongator tRNAMet
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylguanine26 in elongator tRNAMet
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
-
Substrates: the elements necessary for a productive interaction between G26 in nuclear coded yeast tRNAs and the yeast G26 modifying enzyme are located within the core of the tRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in tRNAPhe
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNAPhe
-
Substrates: tRNAPhe from yeast
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in tRNAPhe
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNAPhe
Substrates: tRNAPhe from yeast
Products: -
Products: -
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
Substrates: the efficient dimethylation of guanine26 requires the presence of base-pairs C11*G24 and G10*C25 and a variable loop of five bases within a correct 3D-core of the tRNA molecule. These identity elements probably ensure the correct presentation of methylated m2G26 to the enzyme for the attachment of the second methyl group
Products: -
Products: -
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
Substrates: the efficient dimethylation of guanine26 requires the presence of base-pairs C11*G24 and G10*C25 and a variable loop of five bases within a correct 3D-core of the tRNA molecule. These identity elements probably ensure the correct presentation of methylated m2G26 to the enzyme for the attachment of the second methyl group. The methylated intermediate, and the enzyme dissociates from its tRNA substrate between the two consecutive methylation reactions
Products: -
Products: -
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
Substrates: the elements necessary for a productive interaction between G26 in nuclear coded yeast tRNAs and the yeast G26 modifying enzyme are located within the core of the tRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNAPhe
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNAPhe
-
Substrates: tRNAPhe from yeast, the efficient dimethylation of guanine26 requires the presence of base-pairs C11*G24 and G10*C25 and a variable loop of five bases within a correct 3D-core of the tRNA molecule. These identity elements probably ensure the correct presentation of methylated m2G26 to the enzyme for the attachment of the second methyl group
Products: -
Products: -
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNAPhe
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNAPhe
Substrates: tRNAPhe from yeast
Products: -
Products: -
?
additional information
?
-
Substrates: human TRMT1 independently catalyzes formation of the tRNA:m2G26 or m22G26 modification in a substrate-dependent manner. For TRMT1-mediated tRNA:m22G26 formation, the semiconserved C11:G24 serves as the determinant, and the U10:A25 or G10:C25 base pair is also required, while the size of the variable loop has no effect
Products: -
Products: -
-
additional information
?
-
Substrates: TRMT1 is the primary enzyme responsible for all detectable m2G or m2,2G modifications at position 26 in nucleus- and mitochondrion-encoded tRNAs
Products: -
Products: -
-
additional information
?
-
-
Substrates: in yeast tRNAAsp G26 is unmodified. Successive change of the near surroundings of G26 in this tRNA is performed until G26 becomes modified to N2-dimethylguanine26 tRNA by a tRNA(m2(2)G26)methyltransferase in Xenopus laevis oocytes. In this the two D-stem basepairs C1 -G24, G10-C25 are identified immediately preceding G26 as major identity elements for the dimethylating enzyme modifying G26. Increasing the extra loop in tRNAAsp from four to the more usual five bases influence the global structure of the tRNA such that the mJG26 formation is drastically decreased even if the near region of G26 had the two consensus basepairs. Not only are the two consensus base pairs in the D-stem a prerequisite for G26 modification, but also is any part of the tRNA molecule that influence the 3D-structure important for the recognition between nuclear coded tRNAs and the tRNA(mJG26)methyltransferase
Products: -
Products: -
?
additional information
?
-
Substrates: Ta0997 gene product is a single site-specific Trm1
Products: -
Products: -
?
additional information
?
-
-
Substrates: Ta0997 gene product is a single site-specific Trm1
Products: -
Products: -
?
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
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNA
-
Substrates: the efficient dimethylation of guanine26 requires the presence of base-pairs C11*G24 and G10*C25 and a variable loop of five bases within a correct 3D-core of the tRNA molecule. These identity elements probably ensure the correct presentation of methylated m2G26 to the enzyme for the attachment of the second methyl group
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNALeu(UAG)
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeu(UAG)
S-adenosyl-L-methionine + 2'-O-methylguanine26 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-dimethylguanine26 in elongator tRNAMet
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 2'-O-methylguanine26 in initiator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-dimethylguanine26 in initiator tRNAMet
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylguanine26 in elongator tRNAMet
S-adenosyl-L-methionine + guanine26 in initiator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylguanine26 in initiator tRNAMet
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNALeu(UAG)
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeu(UAG)
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNALeu(UAG)
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeu(UAG)
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNALeu(UAG)
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeu(UAG)
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNALeu(UAG)
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeu(UAG)
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + guanine26 in tRNALeu(UAG)
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeu(UAG)
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylguanine26 in elongator tRNAMet
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylguanine26 in elongator tRNAMet
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylguanine26 in elongator tRNAMet
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylguanine26 in elongator tRNAMet
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylguanine26 in elongator tRNAMet
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
Substrates: the efficient dimethylation of guanine26 requires the presence of base-pairs C11*G24 and G10*C25 and a variable loop of five bases within a correct 3D-core of the tRNA molecule. These identity elements probably ensure the correct presentation of methylated m2G26 to the enzyme for the attachment of the second methyl group
Products: -
Products: -
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
Thermoplasma acidophilum grows optimally at 59°C and pH 1.9
brenda
additional information
-
Thermoplasma acidophilum grows optimally at 59°C and pH 1.9
brenda
additional information
-
Thermoplasma acidophilum grows optimally at 59°C and pH 1.9
-
brenda
additional information
-
Thermoplasma acidophilum grows optimally at 59°C and pH 1.9
-
brenda
additional information
-
Thermoplasma acidophilum grows optimally at 59°C and pH 1.9
-
brenda
additional information
-
Thermoplasma acidophilum grows optimally at 59°C and pH 1.9
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
cytosolic tRNAs with G26 predominantly contain modification m22G26
brenda
mitochondrial tRNAs with G26 predominantly contain modification m2G26, or unmodified G26
brenda
targeting to nucleus or mitochondrion depends on alternate transcriptional start sites
brenda
-
targeting to nucleus or mitochondrion depends on alternate transcriptional start sites
-
brenda
targeting to nucleus or mitochondrion depends on alternate transcriptional start sites
brenda
-
targeting to nucleus or mitochondrion depends on alternate transcriptional start sites
-
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
evolution
Trm1 enzymes can be divided into two types on the basis of their specificity for the target guanosine(s). One is a single-site-specific, which modifies only G26 and is found in eukaryotes and archaea. The second is a multi-site-specific Trm1, which modifies both G26 and G27 and is found in the hyperthermophilic eubacterium, Aquifex aeolicus
evolution
the requirement for C11:G24 and U10:A25 or G10:C25 base pairs in the D-stem for TRMT1-mediated m22G26 modification applies to higher eukaryotic tRNAs in general
evolution
-
Trm1 enzymes can be divided into two types on the basis of their specificity for the target guanosine(s). One is a single-site-specific, which modifies only G26 and is found in eukaryotes and archaea. The second is a multi-site-specific Trm1, which modifies both G26 and G27 and is found in the hyperthermophilic eubacterium, Aquifex aeolicus
-
evolution
-
Trm1 enzymes can be divided into two types on the basis of their specificity for the target guanosine(s). One is a single-site-specific, which modifies only G26 and is found in eukaryotes and archaea. The second is a multi-site-specific Trm1, which modifies both G26 and G27 and is found in the hyperthermophilic eubacterium, Aquifex aeolicus
-
evolution
-
Trm1 enzymes can be divided into two types on the basis of their specificity for the target guanosine(s). One is a single-site-specific, which modifies only G26 and is found in eukaryotes and archaea. The second is a multi-site-specific Trm1, which modifies both G26 and G27 and is found in the hyperthermophilic eubacterium, Aquifex aeolicus
-
evolution
-
Trm1 enzymes can be divided into two types on the basis of their specificity for the target guanosine(s). One is a single-site-specific, which modifies only G26 and is found in eukaryotes and archaea. The second is a multi-site-specific Trm1, which modifies both G26 and G27 and is found in the hyperthermophilic eubacterium, Aquifex aeolicus
-
malfunction
treatment with rapamycin or overexpression of maf1+ reduces tRNA transcription with increase in the m22G26 content of sup-tRNASerUCA and its specific activity for suppression. Mutations in a catalytic subunit of RNAP III associated with hypomyelinating leukodystrophy (HLD) to show that a general decrease in tRNA transcription by another mechanism also increases m22G26 modification efficiency and reverses antisuppression in Schizosaccharomyces pombe. G26 misincorporations are decreased to below 1% in trm1DELTA mutant cells. Expression of trm1+ from a high copy plasmid in trm1DELTA cells restores the misincorporations to higher levels than in wild-type cells
malfunction
human patient cells with disease-associated TRMT1 variants, due to aberrant splicing, reduced TRMT1 expression, and/or loss of TRMT1 activity exhibit reduced levels of tyrosine and serine tRNAs
malfunction
-
treatment with rapamycin or overexpression of maf1+ reduces tRNA transcription with increase in the m22G26 content of sup-tRNASerUCA and its specific activity for suppression. Mutations in a catalytic subunit of RNAP III associated with hypomyelinating leukodystrophy (HLD) to show that a general decrease in tRNA transcription by another mechanism also increases m22G26 modification efficiency and reverses antisuppression in Schizosaccharomyces pombe. G26 misincorporations are decreased to below 1% in trm1DELTA mutant cells. Expression of trm1+ from a high copy plasmid in trm1DELTA cells restores the misincorporations to higher levels than in wild-type cells
-
metabolism
the tRNA modification dimethyl-guanine-26 (m22G26) varies in the efficiency by which it is added to its target tRNAs, in a manner that is dependent on the overall activity rate of RNA polymerase III (RNAP III) that synthesizes the tRNAs. Rapamycin decreases tRNA synthesis in a maf1+-dependent manner in Schizosaccharomyces pombe. Hypomodification of m22G26 is responsible for maf1DELTA antisuppression. RNAP III mutations that decrease tRNA synthesis also increase m22G26 efficiency and tRNA activity
metabolism
-
the tRNA modification dimethyl-guanine-26 (m22G26) varies in the efficiency by which it is added to its target tRNAs, in a manner that is dependent on the overall activity rate of RNA polymerase III (RNAP III) that synthesizes the tRNAs. Rapamycin decreases tRNA synthesis in a maf1+-dependent manner in Schizosaccharomyces pombe. Hypomodification of m22G26 is responsible for maf1DELTA antisuppression. RNAP III mutations that decrease tRNA synthesis also increase m22G26 efficiency and tRNA activity
-
physiological function
the Ta0997 gene product methylates the tRNALeuUAG transcript and 14C-nucleotide analysis reveals that the modified nucleotide is pm22G. Archaeal Trm1 can methylate the tRNALeuUAG transcript, which has a long variable region. In the case of class I tRNAs, archaeal Trm1 is reported to recognize the D-stem and the size of the variable region. Therefore, archaeal Trm1 might be able to recognize the large variable region in the class II tRNAs. Trm1 efficiently methylates both the mature elongator tRNAMet transcript and the precursor with an intron. Archaeal Trm1 does not recognize the anticodon loop. The G modification at position 26 is a mixture of m2G and m22G, which is formed by Trm1
physiological function
after their synthesis by RNAP III, tRNAs are chemically modified by enzymes on multiple of their nucleosides, also involving the enzyme. G26 is modified by N2,N2 dimethylation (m2 2G26) in many tRNAs by the Trm1 methyltransferase. Trm1 is a nuclear enzyme that produces m2 2G26 which likely contributes to proper tRNA folding. N2,N2-dimethyl G26 (m22G26) can enhance tRNA function. Trm1 activity is limiting in the context of increased tRNA production in maf1DELTA cells and its overexpression reverses antisuppression. Of the 36 tRNAs in Schizosaccharomyces pombe that have G26, 27 show significant misincorporation at G26. The extent of G26 misincorporation varies with tRNA identity from 10-80%, G26 misincorporations are due to m22G26 modification. A significant amount of Trm1 substrates are not fully modified in wild-type cells because Trm1 activity is limiting. Hypomodification of m22G26 is responsible for maf1DELTA antisuppression. m22G26 modification debilitates normal base pairing. Efficiency of m22G26 modification responds to growth/nutrient conditions, overview
physiological function
wild-type and catalytic-dead Trm1 are active in an in vivo tRNA-mediated suppression assay and possess RNA strand annealing and dissociation activity in vitro. RNA chaperone La binding to nascent pre-tRNAs decreases Trm1 tRNA dimethylation in vivo and in vitro
physiological function
-
after their synthesis by RNAP III, tRNAs are chemically modified by enzymes on multiple of their nucleosides, also involving the enzyme. G26 is modified by N2,N2 dimethylation (m2 2G26) in many tRNAs by the Trm1 methyltransferase. Trm1 is a nuclear enzyme that produces m2 2G26 which likely contributes to proper tRNA folding. N2,N2-dimethyl G26 (m22G26) can enhance tRNA function. Trm1 activity is limiting in the context of increased tRNA production in maf1DELTA cells and its overexpression reverses antisuppression. Of the 36 tRNAs in Schizosaccharomyces pombe that have G26, 27 show significant misincorporation at G26. The extent of G26 misincorporation varies with tRNA identity from 10-80%, G26 misincorporations are due to m22G26 modification. A significant amount of Trm1 substrates are not fully modified in wild-type cells because Trm1 activity is limiting. Hypomodification of m22G26 is responsible for maf1DELTA antisuppression. m22G26 modification debilitates normal base pairing. Efficiency of m22G26 modification responds to growth/nutrient conditions, overview
-
physiological function
-
wild-type and catalytic-dead Trm1 are active in an in vivo tRNA-mediated suppression assay and possess RNA strand annealing and dissociation activity in vitro. RNA chaperone La binding to nascent pre-tRNAs decreases Trm1 tRNA dimethylation in vivo and in vitro
-
physiological function
-
the Ta0997 gene product methylates the tRNALeuUAG transcript and 14C-nucleotide analysis reveals that the modified nucleotide is pm22G. Archaeal Trm1 can methylate the tRNALeuUAG transcript, which has a long variable region. In the case of class I tRNAs, archaeal Trm1 is reported to recognize the D-stem and the size of the variable region. Therefore, archaeal Trm1 might be able to recognize the large variable region in the class II tRNAs. Trm1 efficiently methylates both the mature elongator tRNAMet transcript and the precursor with an intron. Archaeal Trm1 does not recognize the anticodon loop. The G modification at position 26 is a mixture of m2G and m22G, which is formed by Trm1
-
physiological function
-
the Ta0997 gene product methylates the tRNALeuUAG transcript and 14C-nucleotide analysis reveals that the modified nucleotide is pm22G. Archaeal Trm1 can methylate the tRNALeuUAG transcript, which has a long variable region. In the case of class I tRNAs, archaeal Trm1 is reported to recognize the D-stem and the size of the variable region. Therefore, archaeal Trm1 might be able to recognize the large variable region in the class II tRNAs. Trm1 efficiently methylates both the mature elongator tRNAMet transcript and the precursor with an intron. Archaeal Trm1 does not recognize the anticodon loop. The G modification at position 26 is a mixture of m2G and m22G, which is formed by Trm1
-
physiological function
-
the Ta0997 gene product methylates the tRNALeuUAG transcript and 14C-nucleotide analysis reveals that the modified nucleotide is pm22G. Archaeal Trm1 can methylate the tRNALeuUAG transcript, which has a long variable region. In the case of class I tRNAs, archaeal Trm1 is reported to recognize the D-stem and the size of the variable region. Therefore, archaeal Trm1 might be able to recognize the large variable region in the class II tRNAs. Trm1 efficiently methylates both the mature elongator tRNAMet transcript and the precursor with an intron. Archaeal Trm1 does not recognize the anticodon loop. The G modification at position 26 is a mixture of m2G and m22G, which is formed by Trm1
-
physiological function
-
the Ta0997 gene product methylates the tRNALeuUAG transcript and 14C-nucleotide analysis reveals that the modified nucleotide is pm22G. Archaeal Trm1 can methylate the tRNALeuUAG transcript, which has a long variable region. In the case of class I tRNAs, archaeal Trm1 is reported to recognize the D-stem and the size of the variable region. Therefore, archaeal Trm1 might be able to recognize the large variable region in the class II tRNAs. Trm1 efficiently methylates both the mature elongator tRNAMet transcript and the precursor with an intron. Archaeal Trm1 does not recognize the anticodon loop. The G modification at position 26 is a mixture of m2G and m22G, which is formed by Trm1
-
Show AA Sequence and Transmembrane Helices (6582 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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop method, crystal structures of Trm1 from Pyrococcus horikoshii liganded with S-adenosyl-l-methionine or S-adenosyl-l-homocysteine
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S467L
complete loss of enzyme activity in vitro against trm1 yeast tRNA
D201A
additional information
D201A
loss of activity on both nuclear- and mitochondrial-encoded tRNAs
D201A
-
loss of activity on both nuclear- and mitochondrial-encoded tRNAs
-
additional information
comparatively short N- or C-terminal deletions from the 570 amino acid long Trm1 polypeptide decreased or eliminated the enzyme activity. The first 27 N-terminal amino acids in rTrmp1 are not needed for G26 modification activity in vitro or in vivo. DELTAC5aa causes the in vitro modification activity to drastically decrease to 27% of the wild-type rate. Additional deletions up to DELTA30aa further lower the activity to about 7% of the wild-type value. In DELTA10aa an increase of the N2-methylguanine26 relative to N2-dimethylguanine26 tRNA is observed, but with further C-terminal deletions the monomethylation activity is also severely lowered
additional information
-
comparatively short N- or C-terminal deletions from the 570 amino acid long Trm1 polypeptide decreased or eliminated the enzyme activity. The first 27 N-terminal amino acids in rTrmp1 are not needed for G26 modification activity in vitro or in vivo. DELTAC5aa causes the in vitro modification activity to drastically decrease to 27% of the wild-type rate. Additional deletions up to DELTA30aa further lower the activity to about 7% of the wild-type value. In DELTA10aa an increase of the N2-methylguanine26 relative to N2-dimethylguanine26 tRNA is observed, but with further C-terminal deletions the monomethylation activity is also severely lowered
additional information
generation of a trm1DELTA knockout mutant
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, the purified enzyme can be stored for several months without loss of activity
-
frozen in small portions, enzyme maintains activity for at least several months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21 (DE3) Rosetta 2
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli and the His-tagged Trm1 protein
expression in Escherichia coli
gene Ta0997, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain BL21 (DE3) Rosetta 2
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ihsanawati; Nishimoto, M.; Higashijima, K.; Shirouzu, M.; Grosjean, H.; Bessho, Y.; Yokoyama, S.
Crystal Structure of tRNA N(2),N(2)-Guanosine Dimethyltransferase Trm1 from Pyrococcus horikoshii
J. Mol. Biol.
383
871-884
2008
Pyrococcus horikoshii (O59493)
brenda
Edqvist, J.; Blomqvist, K.; Straby, K.B.
Structural elements in yeast tRNAs required for homologous modification of guanosine-26 into dimethylguanosine-26 by the yeast Trm1 tRNA-modifying enzyme
Biochemistry
33
9546-9551
1994
Saccharomyces cerevisiae
brenda
Liu, J.; Zhou, G.Q.; Strabym K.B.
Caenorhabditis elegans ZC376.5 encodes a tRNA (m2/2G(26))dimethyltransferance in which (246)arginine is important for the enzyme activity
Gene
226
73-81
1999
Caenorhabditis elegans (Q23270), Caenorhabditis elegans, Saccharomyces cerevisiae (P15565), Saccharomyces cerevisiae
brenda
Constantinesco, F.; Motorin, Y.; Grosjean, H.
Characterisation and enzymatic properties of tRNA(guanine 26, N2,N2)-dimethyltransferase (Trm1p) from Pyrococcus furiosus
J. Mol. Biol.
291
375-392
1999
Pyrococcus furiosus
brenda
Edqvist, J.; Grosjean, H.; Straby, K.B.
Identity elements for N2-dimethylation of guanosine-26 in yeast tRNAs
Nucleic Acids Res.
20
6575-6581
1992
Saccharomyces cerevisiae
brenda
Constantinesco, F.; Benachenhou, N.; Motorin, Y.; Grosjean, H.
The tRNA(guanine-26,N2-N2) methyltransferase (Trm1) from the hyperthermophilic archaeon Pyrococcus furiosus: cloning, sequencing of the gene and its expression in Escherichia coli
Nucleic Acids Res.
26
3753-3761
1998
Pyrococcus furiosus (P15565), Pyrococcus furiosus
brenda
Liu, J.; Liu, J.; Straby, K.B.
Point and deletion mutations eliminate one or both methyl group transfers catalysed by the yeast TRM1 encoded tRNA (m22G26)dimethyltransferase
Nucleic Acids Res.
26
5102-5108
1998
Saccharomyces cerevisiae (P15565), Saccharomyces cerevisiae
brenda
Kawamura, T.; Anraku, R.; Hasegawa, T.; Tomikawa, C.; Hori, H.
Transfer RNA methyltransferases from Thermoplasma acidophilum, a thermoacidophilic archaeon
Int. J. Mol. Sci.
16
91-113
2015
Thermoplasma acidophilum (P57706), Thermoplasma acidophilum, Thermoplasma acidophilum AMRC-C165 (P57706), Thermoplasma acidophilum ATCC 25905 (P57706), Thermoplasma acidophilum JCM 9062 (P57706), Thermoplasma acidophilum NBRC 15155 (P57706)
brenda
Arimbasseri, A.; Blewett, N.; Iben, J.; Lamichhane, T.; Cherkasova, V.; Hafner, M.; Maraia, R.
RNA polymerase III output is functionally linked to tRNA dimethyl-G26 modification
PLoS Genet.
11
e1005671
2015
Schizosaccharomyces pombe (Q9P804), Schizosaccharomyces pombe 972 (Q9P804)
brenda
Zhang, K.; Manning, A.C.; Lentini, J.M.; Howard, J.; Dalwigk, F.; Maroofian, R.; Efthymiou, S.; Chan, P.; Eliseev, S.I.; Yang, Z.; Chang, H.; Karimiani, E.G.; Bakhshoodeh, B.; Houlden, H.; Kaiser, S.M.; Lowe, T.M.; Fu, D.
Human TRMT1 and TRMT1L paralogs ensure the proper modification state, stability, and function of tRNAs
Cell Rep.
44
115092
2025
Homo sapiens (Q9NXH9)
brenda
Porat, J.; Vakiloroayaei, A.; Remnant, B.; Talebi, M.; Cargill, T.; Bayfield, M.
Crosstalk between the tRNA methyltransferase Trm1 and RNA chaperone La influences eukaryotic tRNA maturation
J. Biol. Chem.
299
105326
2023
Schizosaccharomyces pombe (Q9P804), Schizosaccharomyces pombe 972 (Q9P804)
brenda
Xiong, Q.P.; Li, J.; Li, H.; Huang, Z.X.; Dong, H.; Wang, E.D.; Liu, R.J.
Human TRMT1 catalyzes m2G or m22G formation on tRNAs in a substrate-dependent manner
Sci. China Life Sci.
66
2295-2309
2023
Homo sapiens (Q9NXH9)
brenda
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