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2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNAArg
2 S-adenosyl-L-homocysteine + adenine57/N1-methyladenine58 in tRNAArg
modified mini-tRNAAsp substrate, PabTrmI recognizes and methylates only A58 in mini-tRNAArgTCT containing the G57A58A59U60 sequence
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2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNAAsp
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNAAsp
additional information
?
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2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
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2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
the solvent accessibility of the S-adenosyl-L-methionine pocket is not affected by the tRNA, thereby enabling S-adenosyl-L-homocysteine to be replaced by S-adenosyl-L-methionine without prior release of monomethylated tRNA
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?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
the solvent accessibility of the S-adenosyl-L-methionine pocket is not affected by the tRNA, thereby enabling S-adenosyl-L-homocysteine to be replaced by S-adenosyl-L-methionine without prior release of monomethylated tRNA
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?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
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?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNAAsp
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNAAsp
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?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNAAsp
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNAAsp
the presence of adenine at position 59 in Pyrococcus abyssi tRNA(Asp) is important for the multi-site specificity of the archaeal enzyme at both positions 57 and 58 in tRNAAsp. His78 near the active site is important for efficient catalysis
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2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNAAsp
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNAAsp
modified mini-tRNAAsp substrate, PabTrmI recognizes and methylates both A57 and A58 in mini-tRNAAsp containing the A57A58A59U60 sequence
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-
?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNAAsp
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNAAsp
modified mini-tRNAAsp substrate, PabTrmI recognizes and methylates both A57 and A58 in mini-tRNAAsp containing the A57A58A59U60 sequence
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-
?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNAAsp
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNAAsp
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?
additional information
?
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methylation occurs at position 58 when position 57 contains a methylated adenine, an adenine derivative or guanine, whereas the methylation at position 57 strictly requires adenine 58 to proceed efficiently. This supports our previous conclusion that A57 is methylated before A58 in tRNAs containing the A57A58A59 sequence
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?
additional information
?
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methylation occurs at position 58 when position 57 contains a methylated adenine, an adenine derivative or guanine, whereas the methylation at position 57 strictly requires adenine 58 to proceed efficiently. This supports our previous conclusion that A57 is methylated before A58 in tRNAs containing the A57A58A59 sequence
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?
additional information
?
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in most organisms, the widely conserved 1-methyladenosine58 (m1A58) tRNA modification is catalyzed by S-adenosyl-L-methionine-dependent site-specific enzyme TrmI. In archaea, TrmI also methylates the adjacent adenine 57, m1A57 being an obligatory intermediate of 1-methyl-inosine57 formation, multi-site specificity mechanism, overview
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?
additional information
?
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in most organisms, the widely conserved 1-methyladenosine58 (m1A58) tRNA modification is catalyzed by S-adenosyl-L-methionine-dependent site-specific enzyme TrmI. In archaea, TrmI also methylates the adjacent adenine 57, m1A57 being an obligatory intermediate of 1-methyl-inosine57 formation, multi-site specificity mechanism, overview
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?
additional information
?
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construction of three oligoribonucleotide substrates of Pyrococcus abyssi TrmI containing a fluorescent 2-aminopurine at the two target positions 57 and 58, analysis of RNA binding kinetics and methylation reactions by stopped-flow and mass spectrometry, overview. PabTrmI does not modify 2-aminopurine but methylates the adjacent target adenine. 2-Aminopurine seriously impairs the methylation of A57 but not A58, confirming that PabTrmI methylates efficiently the first adenine of the A57A58A59 sequence
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?
additional information
?
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construction of three oligoribonucleotide substrates of Pyrococcus abyssi TrmI containing a fluorescent 2-aminopurine at the two target positions 57 and 58, analysis of RNA binding kinetics and methylation reactions by stopped-flow and mass spectrometry, overview. PabTrmI does not modify 2-aminopurine but methylates the adjacent target adenine. 2-Aminopurine seriously impairs the methylation of A57 but not A58, confirming that PabTrmI methylates efficiently the first adenine of the A57A58A59 sequence
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-
?
additional information
?
-
methylation occurs at position 58 when position 57 contains a methylated adenine, an adenine derivative or guanine, whereas the methylation at position 57 strictly requires adenine 58 to proceed efficiently. This supports our previous conclusion that A57 is methylated before A58 in tRNAs containing the A57A58A59 sequence
-
-
?
additional information
?
-
in most organisms, the widely conserved 1-methyladenosine58 (m1A58) tRNA modification is catalyzed by S-adenosyl-L-methionine-dependent site-specific enzyme TrmI. In archaea, TrmI also methylates the adjacent adenine 57, m1A57 being an obligatory intermediate of 1-methyl-inosine57 formation, multi-site specificity mechanism, overview
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?
additional information
?
-
construction of three oligoribonucleotide substrates of Pyrococcus abyssi TrmI containing a fluorescent 2-aminopurine at the two target positions 57 and 58, analysis of RNA binding kinetics and methylation reactions by stopped-flow and mass spectrometry, overview. PabTrmI does not modify 2-aminopurine but methylates the adjacent target adenine. 2-Aminopurine seriously impairs the methylation of A57 but not A58, confirming that PabTrmI methylates efficiently the first adenine of the A57A58A59 sequence
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-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
additional information
?
-
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
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-
-
?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
the solvent accessibility of the S-adenosyl-L-methionine pocket is not affected by the tRNA, thereby enabling S-adenosyl-L-homocysteine to be replaced by S-adenosyl-L-methionine without prior release of monomethylated tRNA
-
-
?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
the solvent accessibility of the S-adenosyl-L-methionine pocket is not affected by the tRNA, thereby enabling S-adenosyl-L-homocysteine to be replaced by S-adenosyl-L-methionine without prior release of monomethylated tRNA
-
-
?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
-
-
-
?
additional information
?
-
in most organisms, the widely conserved 1-methyladenosine58 (m1A58) tRNA modification is catalyzed by S-adenosyl-L-methionine-dependent site-specific enzyme TrmI. In archaea, TrmI also methylates the adjacent adenine 57, m1A57 being an obligatory intermediate of 1-methyl-inosine57 formation, multi-site specificity mechanism, overview
-
-
?
additional information
?
-
-
in most organisms, the widely conserved 1-methyladenosine58 (m1A58) tRNA modification is catalyzed by S-adenosyl-L-methionine-dependent site-specific enzyme TrmI. In archaea, TrmI also methylates the adjacent adenine 57, m1A57 being an obligatory intermediate of 1-methyl-inosine57 formation, multi-site specificity mechanism, overview
-
-
?
additional information
?
-
in most organisms, the widely conserved 1-methyladenosine58 (m1A58) tRNA modification is catalyzed by S-adenosyl-L-methionine-dependent site-specific enzyme TrmI. In archaea, TrmI also methylates the adjacent adenine 57, m1A57 being an obligatory intermediate of 1-methyl-inosine57 formation, multi-site specificity mechanism, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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additional information
PabTrmI methylates efficiently the first adenine of the A57A58A59 sequence. m1A58 formation triggers RNA release. A model of the protein-tRNA complex shows both target adenines in proximity of S-adenosyl-L-methionine and emphasizes no major tRNA conformational change except base flipping during the reaction. The solvent accessibility of the S-adenosyl-L-methionine pocket is not affected by the tRNA, thereby enabling S-adenosyl-L-homocysteine to be replaced by S-adenosyl-L-methionine without prior release of monomethylated tRNA. Dynamics of RNA binding by PabTrmI in the presence and absence of S-adenosyl-L-methionine, structural model of PabTrmI in complex with tRNA, overview
additional information
-
PabTrmI methylates efficiently the first adenine of the A57A58A59 sequence. m1A58 formation triggers RNA release. A model of the protein-tRNA complex shows both target adenines in proximity of S-adenosyl-L-methionine and emphasizes no major tRNA conformational change except base flipping during the reaction. The solvent accessibility of the S-adenosyl-L-methionine pocket is not affected by the tRNA, thereby enabling S-adenosyl-L-homocysteine to be replaced by S-adenosyl-L-methionine without prior release of monomethylated tRNA. Dynamics of RNA binding by PabTrmI in the presence and absence of S-adenosyl-L-methionine, structural model of PabTrmI in complex with tRNA, overview
additional information
-
PabTrmI methylates efficiently the first adenine of the A57A58A59 sequence. m1A58 formation triggers RNA release. A model of the protein-tRNA complex shows both target adenines in proximity of S-adenosyl-L-methionine and emphasizes no major tRNA conformational change except base flipping during the reaction. The solvent accessibility of the S-adenosyl-L-methionine pocket is not affected by the tRNA, thereby enabling S-adenosyl-L-homocysteine to be replaced by S-adenosyl-L-methionine without prior release of monomethylated tRNA. Dynamics of RNA binding by PabTrmI in the presence and absence of S-adenosyl-L-methionine, structural model of PabTrmI in complex with tRNA, overview
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Roovers, M.; Wouters, J.; Bujnicki, J.M.; Tricot, C.; Stalon, V.; Grosjean, H.; Droogmans, L.
A primordial RNA modification enzyme: the case of tRNA (m1A) methyltransferase
Nucleic Acids Res.
32
465-476
2004
Pyrococcus abyssi (Q9V1J7), Pyrococcus abyssi, Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543 (Q9V1J7)
brenda
Guelorget, A.; Roovers, M.; Gurineau, V.; Barbey, C.; Li, X.; Golinelli-Pimpaneau, B.
Insights into the hyperthermostability and unusual region-specificity of archaeal Pyrococcus abyssi tRNA m1A57/58 methyltransferase
Nucleic Acids Res.
38
6206-6218
2010
Pyrococcus abyssi (Q9V1J7), Pyrococcus abyssi
brenda
Hamdane, D.; Guelorget, A.; Gurineau, V.; Golinelli-Pimpaneau, B.
Dynamics of RNA modification by a multi-site-specific tRNA methyltransferase
Nucleic Acids Res.
42
11697-11706
2015
Pyrococcus abyssi (Q9V1J7), Pyrococcus abyssi, Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543 (Q9V1J7)
brenda