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2 S-adenosyl-L-methionine + guanine26 in elongator tRNAMet
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in elongator tRNAMet
2 S-adenosyl-L-methionine + guanine26 in initiator tRNAMet
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in initiator tRNAMet
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
4 S-adenosyl-L-methionine + guanine26 in initiator tRNAMet
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in initiator tRNAMet
m2G26 and m22G26 are formed by Trm1
-
-
?
4 S-adenosyl-L-methionine + guanine26 in prolongator tRNAMet
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in prolongator tRNAMet
m2G26 and m22G26 are formed by Trm1
-
-
?
4 S-adenosyl-L-methionine + guanine26 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
4 S-adenosyl-L-methionine + guanine26 in tRNALeuCAA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeuCAA
-
-
-
-
?
4 S-adenosyl-L-methionine + guanine26 in tRNALeuTAG
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeuTAG
-
-
-
-
?
4 S-adenosyl-L-methionine + guanine26 in tRNASerUCA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNASerUCA
-
-
-
-
?
S-adenosyl-L-methionine + 2'-O-methylguanine26 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-dimethylguanine26 in elongator tRNAMet
-
-
-
?
S-adenosyl-L-methionine + 2'-O-methylguanine26 in initiator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-dimethylguanine26 in initiator tRNAMet
-
-
-
?
S-adenosyl-L-methionine + guanine26 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylguanine26 in elongator tRNAMet
-
-
-
?
S-adenosyl-L-methionine + guanine26 in elongator tRNAMet
S-adenosyl-L-homocysteine + N2-methylguanine26 in elongator tRNAMet
-
-
-
?
S-adenosyl-L-methionine + guanine26 in initiator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylguanine26 in initiator tRNAMet
-
-
-
?
S-adenosyl-L-methionine + guanine26 in initiator tRNAMet
S-adenosyl-L-homocysteine + N2-methylguanine26 in initiator tRNAMet
-
-
-
?
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
additional information
?
-
2 S-adenosyl-L-methionine + guanine26 in elongator tRNAMet
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in elongator tRNAMet
-
-
-
?
2 S-adenosyl-L-methionine + guanine26 in elongator tRNAMet
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in elongator tRNAMet
-
-
-
-
?
2 S-adenosyl-L-methionine + guanine26 in initiator tRNAMet
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in initiator tRNAMet
-
-
-
?
2 S-adenosyl-L-methionine + guanine26 in initiator tRNAMet
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in initiator tRNAMet
-
-
-
-
?
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 in tRNA
-
-
-
?
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 in tRNA
-
-
-
?
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 in tRNA
-
-
-
?
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
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
-
-
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNA
-
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
-
-
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNA
-
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
-
-
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNA
-
-
-
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNA
-
-
-
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNA
-
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
-
-
?
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNA
wild-type enzyme produces 94% N2-dimethylguanine26 tRNA and 6% N2-methylguanine26 in 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 tRNALeu(UAG)
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeu(UAG)
-
-
-
-
?
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 tRNALeu(UAG)
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeu(UAG)
-
-
-
?
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 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
tRNAPhe from yeast
-
-
?
2 S-adenosyl-L-methionine + guanine26 in tRNAPhe
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNAPhe
-
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
-
-
?
4 S-adenosyl-L-methionine + guanine26 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
G26 is modified by N2,N2-dimethylation in many tRNAs by the Trm1 methyltransferase
-
-
?
4 S-adenosyl-L-methionine + guanine26 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
-
-
?
4 S-adenosyl-L-methionine + guanine26 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
G modification at position 26 is a mixture of m2G and m22G generated by Trm1
-
-
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
-
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
-
-
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
-
-
-
?
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
-
tRNAPhe from yeast
-
-
?
S-adenosyl-L-methionine + guanine26 in tRNAPhe
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNAPhe
tRNAPhe from yeast
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
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
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
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
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
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
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
-
-
?
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
tRNAPhe from yeast
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNAPhe
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNAPhe
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme Trm1 is single site-specific
-
-
?
additional information
?
-
the enzyme Trm1 is single site-specific
-
-
?
additional information
?
-
Ta0997 gene product is a single site-specific Trm1
-
-
-
additional information
?
-
-
Ta0997 gene product is a single site-specific Trm1
-
-
-
additional information
?
-
Ta0997 gene product is a single site-specific Trm1
-
-
-
additional information
?
-
Ta0997 gene product is a single site-specific Trm1
-
-
-
additional information
?
-
Ta0997 gene product is a single site-specific Trm1
-
-
-
additional information
?
-
Ta0997 gene product is a single site-specific Trm1
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
-
?
2 S-adenosyl-L-methionine + guanine26 in tRNALeu(UAG)
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeu(UAG)
4 S-adenosyl-L-methionine + guanine26 in initiator tRNAMet
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in initiator tRNAMet
m2G26 and m22G26 are formed by Trm1
-
-
?
4 S-adenosyl-L-methionine + guanine26 in prolongator tRNAMet
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in prolongator tRNAMet
m2G26 and m22G26 are formed by Trm1
-
-
?
4 S-adenosyl-L-methionine + guanine26 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
4 S-adenosyl-L-methionine + guanine26 in tRNALeuCAA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeuCAA
-
-
-
-
?
4 S-adenosyl-L-methionine + guanine26 in tRNALeuTAG
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeuTAG
-
-
-
-
?
4 S-adenosyl-L-methionine + guanine26 in tRNASerUCA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNASerUCA
-
-
-
-
?
S-adenosyl-L-methionine + 2'-O-methylguanine26 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-dimethylguanine26 in elongator tRNAMet
-
-
-
?
S-adenosyl-L-methionine + 2'-O-methylguanine26 in initiator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-dimethylguanine26 in initiator tRNAMet
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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 in tRNA
-
-
-
?
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 in tRNA
-
-
-
?
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 in 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 tRNALeu(UAG)
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeu(UAG)
-
-
-
?
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 tRNALeu(UAG)
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeu(UAG)
-
-
-
?
2 S-adenosyl-L-methionine + guanine26 in tRNALeu(UAG)
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeu(UAG)
-
-
-
?
4 S-adenosyl-L-methionine + guanine26 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
G26 is modified by N2,N2-dimethylation in many tRNAs by the Trm1 methyltransferase
-
-
?
4 S-adenosyl-L-methionine + guanine26 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
G modification at position 26 is a mixture of m2G and m22G generated by Trm1
-
-
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
-
-
-
?
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
-
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
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
-
-
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?
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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
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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
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evolution
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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
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evolution
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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
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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
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malfunction
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little changes occur in the relative levels of different tRNAs in maf1DELTA cells. By contrast, the efficiency of N2,N2-dimethyl G26 modification on certain tRNAs is decreased in response to maf1-deletion and is associated with antisuppression
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
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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
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metabolism
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global tRNA gene activation occurs with derepression of RNA polymerase III via maf1-deletion and is accompanied by a paradoxical loss of tRNA-mediated nonsense suppressor activity, manifested as an antisuppression phenotype. maf1-Antisuppression also occurs in the fission yeast amidst general activation of RNA polymerase III. Dimethyl-guanine-26 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 polyymerase III. Overexpression of Trm1, which produces the N2,N2-dimethyl G26 modification, reverses maf1-antisuppression. Competition by increased tRNA levels in maf1DELTA cells leads to N2,N2-dimethyl G26 hypomodification due to limiting Trm1, reducing the activity of suppressor-tRNASerUCA and accounting for antisuppression
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
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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
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physiological function
initiator tRNAMet from Thermoplasma acidophilum contains the m22G26 modification in addition to m2G26, the TrmI activity is responsible for these modifications
physiological function
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the N2,N2-dimethyl G26 modification activates the tRNA for function to translate the code. The N2,N2-dimethyl G26 modification is required for the suppressor activity of sup-tRNASerUCA. The enzyme activity is regulated by nutrient/growth conditions
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
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
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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
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physiological function
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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
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physiological function
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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
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physiological function
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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
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physiological function
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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
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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
Saccharomyces cerevisiae (P15565), Saccharomyces cerevisiae, Caenorhabditis elegans (Q23270), Caenorhabditis elegans
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
2014
Thermoplasma acidophilum, Thermoplasma acidophilum (P57706), Thermoplasma acidophilum HO-62
brenda
Arimbasseri, A.G.; Blewett, N.H.; Iben, J.R.; Lamichhane, T.N.; Cherkasova, V.; Hafner, M.; Maraia, R.J.
RNA polymerase III output is functionally linked to tRNA dimethyl-G26 modification
PLoS Genet.
11
e1005671
2015
Schizosaccharomyces pombe
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 JCM 9062 (P57706), Thermoplasma acidophilum AMRC-C165 (P57706), Thermoplasma acidophilum ATCC 25905 (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