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Literature summary for 2.1.1.219 extracted from

  • Hamdane, D.; Guelorget, A.; Guérineau, V.; Golinelli-Pimpaneau, B.
    Dynamics of RNA modification by a multi-site-specific tRNA methyltransferase (2015), Nucleic Acids Res., 42, 11697-11706.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.219

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of C-terminally His6-tagged enzyme Pyrococcus abyssi

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state fluorescent assay and stopped-flow kinetics with 2-aminopurine-modifed tRNA substrates, , overview Pyrococcus abyssi

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Pyrococcus abyssi

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA Pyrococcus abyssi 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-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
-
 ?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543 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-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
-
 ?
additional information Pyrococcus abyssi 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 Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543 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 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Pyrococcus abyssi Q9V1J7
-
-
Pyrococcus abyssi Q9V1J7 gene PAB0283 or trmI
-
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543 Q9V1J7
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrococcus abyssi
recombinant C-terminally His6-tagged enzyme by nickel affiniyt chromatography and gel filtration Pyrococcus abyssi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 S-adenosyl-L-methionine + adenine57/adenine58 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 Pyrococcus abyssi 2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
-
 ?
2 S-adenosyl-L-methionine + adenine57/adenine58 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 Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543 2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
-
 ?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNAArg modified mini-tRNAAsp substrate, PabTrmI recognizes and methylates only A58 in mini-tRNAArgTCT containing the G57A58A59U60 sequence Pyrococcus abyssi 2 S-adenosyl-L-homocysteine + adenine57/N1-methyladenine58 in tRNAArg
-
 ?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNAAsp modified mini-tRNAAsp substrate, PabTrmI recognizes and methylates both A57 and A58 in mini-tRNAAsp containing the A57A58A59U60 sequence Pyrococcus abyssi 2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNAAsp
-
 ?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNAAsp modified mini-tRNAAsp substrate, PabTrmI recognizes and methylates both A57 and A58 in mini-tRNAAsp containing the A57A58A59U60 sequence Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543 2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNAAsp
-
 ?
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 Pyrococcus abyssi ?
-
 ?
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 Pyrococcus abyssi ?
-
 ?
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 Pyrococcus abyssi ?
-
 ?
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 Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543 ?
-
 ?
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 Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543 ?
-
 ?
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 Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543 ?
-
 ?

Synonyms

Synonyms Comment Organism
bi-specific tRNA adenine-N1, A57-A58-methyltransferase
-
 Pyrococcus abyssi
bi-specific tRNA adenine-N1, A57-A58-MTase
-
 Pyrococcus abyssi
PAB0283 protein
-
 Pyrococcus abyssi
PabTrmI
-
 Pyrococcus abyssi
PYRAB04300 locus name Pyrococcus abyssi
tRNA (adenine(57)-N(1)/adenine(58)-N(1))-methyltransferase
-
 Pyrococcus abyssi
tRNA(m1A57/58)-methyltransferase
-
 Pyrococcus abyssi

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Pyrococcus abyssi

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Pyrococcus abyssi

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine dynamics of RNA binding by PabTrmI in the presence and absence of S-adenosyl-L-methionine Pyrococcus abyssi

General Information

General Information Comment Organism
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 Pyrococcus abyssi