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4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNACys
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNACys
m2G26 formation is faster than the m2G27 formation and disruption of the G27-C43 base pair accelerates velocity of the G27 modification. A fraction of native tRNACys has a N2-dimethylguanine26/N2-dimethylguanine27 modification. Initially the N2-methylguanine26 modification occurs, and then the second methyl transfer reaction generates N2-dimethylguanine26. The third methyl transfer reaction modifies guanine 27 to N2-methylguanine27 followed by a fourth methylation of N2-methylguanine27 to N2-dimethylguanine27
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4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNAPhe
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNAPhe
S-adenosyl-L-methionine + guanine26 in mutant tRNATyr
S-adenosyl-L-homocysteine + N2-methylguanine26 in mutant tRNATyr
mutant tRNATyr in which the wilde-type adenine26/guanine27 sequence is substituted with guanine26/adenine27
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S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26/guanine27 in tRNA
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S-adenosyl-L-methionine + guanine26/guanine27 in tRNACys
S-adenosyl-L-homocysteine + N2-methylguanine26/guanine27 in tRNACys
m2G26 formation is faster than the m2G27 formation and disruption of the G27-C43 base pair accelerates velocity of the G27 modification
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S-adenosyl-L-methionine + guanine27 in tRNATyr
S-adenosyl-L-homocysteine + N2-methylguanine27 in tRNATyr
wild-type tRNATyr contains the sequence adenine26/guanine27
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S-adenosyl-L-methionine + N2-dimethylguanine26/guanine27 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-methylguanine27 in tRNA
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?
S-adenosyl-L-methionine + N2-dimethylguanine26/guanine27 in tRNACys
S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-methylguanine27 in tRNACys
m2G26 formation is faster than the m2G27 formation and disruption of the G27-C43 base pair accelerates velocity of the G27 modification
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S-adenosyl-L-methionine + N2-dimethylguanine26/N2-methylguanine27
S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27
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?
S-adenosyl-L-methionine + N2-dimethylguanine26/N2-methylguanine27 in tRNACys
S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNACys
m2G26 formation is faster than the m2G27 formation and disruption of the G27-C43 base pair accelerates velocity of the G27 modification
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?
S-adenosyl-L-methionine + N2-methylguanine26 in mutant tRNATyr
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in mutant tRNATyr
mutant tRNATyr in which the wilde-type adenine26/guanine27 sequence is substituted with guanine26/adenine27
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S-adenosyl-L-methionine + N2-methylguanine26/guanine27 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26/guanine27 in tRNA
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?
S-adenosyl-L-methionine + N2-methylguanine26/guanine27 in tRNACys
S-adenosyl-L-homocysteine + N2-dimethylguanine26/guanine27 in tRNACys
m2G26 formation is faster than the m2G27 formation and disruption of the G27-C43 base pair accelerates velocity of the G27 modification
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?
S-adenosyl-L-methionine + N2-methylguanine27 in tRNATyr
S-adenosyl-L-homocysteine + N2-dimethylguanine27 in tRNATyr
wild-type tRNATyr contains the sequence adenine26/guanine27
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additional information
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4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
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4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
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?
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
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the T-arm in tRNA is the binding site of Trm1, multisite specificity, tRNA-docking modeling, overview
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4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
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?
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNAPhe
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNAPhe
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tRNAPhe from yeast
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4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNAPhe
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNAPhe
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tRNAPhe from yeast
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additional information
?
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Aquifex aeolicus TRm1 may recognize only D-stem structure and guanine26 residue
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additional information
?
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recognition mechanisms of the Trm1 proteins: Aquifex aeolicus Trm1 recognizes the guanine26 and guanine27 bases from the T-arm. In contrast, archaeal and eukaryotic Trm1 proteins recognize the guanine26 base from the D-stem and variable region. The distance between the T-arm and guanine26 (or guanine27) is longer than the distance between the D-stem, variable region, and guanine26. These differences from binding site to the target guanine base(s) may decide the multisite or single site recognition of the Trm1 proteins
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additional information
?
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recognition mechanisms of the Trm1 proteins: Aquifex aeolicus Trm1 recognizes the guanine26 and guanine27 bases from the T-arm. In contrast, archaeal and eukaryotic Trm1 proteins recognize the guanine26 base from the D-stem and variable region. The distance between the T-arm and guanine26 (or guanine27) is longer than the distance between the D-stem, variable region, and guanine26. These differences from binding site to the target guanine base(s) may decide the multisite or single site recognition of the Trm1 proteins
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additional information
?
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yeast tRNAPhe and Escherichia coli tRNALeu transcripts are methylated. In contrast, Escherichia coli tRNASer is not methylated, because this tRNA possesses adenine26 sequence instead of guanine26
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additional information
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Trm1 catalyzes methyl transfers to class II tRNAs as well as all class I tRNAs, the size and sequence of the variable region are not recognized by Aquifex aeolicus Trm1, all tRNA transcripts are methylated. tRNA recognition mechanism of multisite specific Trm1, Asp132 is a catalytic center, structure-function analysis, overview
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4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26/guanine27 in tRNA
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S-adenosyl-L-methionine + N2-dimethylguanine26/guanine27 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-methylguanine27 in tRNA
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?
S-adenosyl-L-methionine + N2-dimethylguanine26/N2-methylguanine27
S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27
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?
S-adenosyl-L-methionine + N2-methylguanine26/guanine27 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26/guanine27 in tRNA
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?
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
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?
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
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?
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.00009
guanine26 in mutant tRNATyr
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0.00008 - 0.00017
guanine27 in tRNATyr
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0.00017 - 0.33
S-adenosyl-L-methionine
0.00009
guanine26 in mutant tRNATyr
pH 7.5, 55°C, mutant tRNATyr in which the wilde-type adenine26/guanine27 sequence is substituted with guanine26/adenine27
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0.00009
guanine26 in mutant tRNATyr
pH 7.5, 55°C, mutant tRNATyr in which the wilde-type adenine26/guanine27 sequence is substituted with guanine26/adenine27, additional point mutation C43U
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0.00008
guanine27 in tRNATyr
pH 7.5, 55°C, tRNA Tyr with wild-type sequence adenine26/guanine27 and mutation C43U
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0.00017
guanine27 in tRNATyr
pH 7.5, 55°C, wild-type tRNATyr contains the sequence adenine26/guanine27
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0.00017
S-adenosyl-L-methionine
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pH 7.5, 55°C, recombinant mutant I85A
0.00017
S-adenosyl-L-methionine
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pH 7.5, 55°C, recombinant wild-type enzyme
0.0002
S-adenosyl-L-methionine
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pH 7.5, 55°C, recombinant mutant I65A
0.0003
S-adenosyl-L-methionine
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pH 7.5, 55°C, recombinant mutant E6A
0.0003
S-adenosyl-L-methionine
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pH 7.5, 55°C, recombinant mutant N29A
0.00067
S-adenosyl-L-methionine
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pH 7.5, 55°C, recombinant mutants L60A, F140A, and E113A
0.0008
S-adenosyl-L-methionine
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pH 7.5, 55°C, recombinant mutant F134A
0.0013
S-adenosyl-L-methionine
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pH 7.5, 55°C, recombinant mutant D130A
0.023
S-adenosyl-L-methionine
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pH 7.5, 55°C, recombinant mutant F27A
0.045
S-adenosyl-L-methionine
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pH 7.5, 55°C, recombinant mutant R66A
0.33
S-adenosyl-L-methionine
-
pH 7.5, 55°C, recombinant mutant D84A
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D130A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D132A
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site-directed mutagenesis, inactive mutant
D84A
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site-directed mutagenesis, almost inactive mutant
E113A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E6A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F134A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F140A
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site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
F27A
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site-directed mutagenesis, almost inactive mutant
H110A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H219A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H274A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
I65A
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site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
I85A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K170A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K283A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L60A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N29A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R179A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R192A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R31A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R36A
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site-directed mutagenesis, inactive mutant
R66A
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site-directed mutagenesis, almost inactive mutant
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Awai, T.; Kimura, S.; Tomikawa, C.; Ochi, A.; Ihsanawati, A.; Bessho, Y.; Yokoyama, S.; Ohno, S.; Nishikawa, K.; Yokogawa, T.; Suzuki, T.; Hori, H.
Aquifex aeolicus tRNA (N2,N2-guanine)-dimethyltransferase (Trm1) catalyzes transfer of methyl groups not only to guanine 26 but also to guanine 27 in tRNA
J. Biol. Chem.
284
20467-20478
2009
Aquifex aeolicus (O67010), Aquifex aeolicus
brenda
Takeda, H.; Hori, H.; Endo, Y.
Identification of Aquifex aeolicus tRNA (m2(2)G26) methyltransferase gene
Nucleic Acids Res. Suppl.
2002
229-230
2002
Aquifex aeolicus
brenda
Awai, T.; Takehara, T.; Takeda, H.; Hori, H.
Aquifex aeolicus Trm1[tRNA (m2(2)G26) methyltransferase] has a novel recognition mechanism of the substrate RNA
Nucleic Acids Symp. Ser.
49
303-304
2005
Aquifex aeolicus
brenda
Awai, T.; Ochi, A.; Ihsanawati, A.; Sengoku, T.; Hirata, A.; Bessho, Y.; Yokoyama, S.; Hori, H.
Substrate tRNA recognition mechanism of a multisite-specific tRNA methyltransferase, Aquifex aeolicus Trm1, based on the X-ray crystal structure
J. Biol. Chem.
286
35236-35246
2011
Aquifex aeolicus
brenda
Motorin, Y.; Burhenne, J.; Teimer, R.; Koynov, K.; Willnow, S.; Weinhold, E.; Helm, M.
Expanding the chemical scope of RNA:methyltransferases to site-specific alkynylation of RNA for click labeling
Nucleic Acids Res.
39
1943-1952
2011
Pyrococcus furiosus
brenda