Enzymes
| UniProtKB help_outline | 1 proteins |
Reaction participants Show >> << Hide
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Namehelp_outline
adenosine32 in tRNA
Identifier
RHEA-COMP:14779
Reactive part
help_outline
- Name help_outline AMP residue Identifier CHEBI:74411 Charge -1 Formula C10H11N5O6P Positionhelp_outline 32 SMILEShelp_outline NC1=NC=NC2=C1N=CN2[C@@H]3O[C@H](COP(=O)(*)[O-])[C@@H](O*)[C@H]3O 2D coordinates Mol file for the small molecule Search links Involved in 40 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline S-adenosyl-L-methionine Identifier CHEBI:59789 Charge 1 Formula C15H23N6O5S InChIKeyhelp_outline MEFKEPWMEQBLKI-AIRLBKTGSA-O SMILEShelp_outline C[S+](CC[C@H]([NH3+])C([O-])=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 868 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
2'-O-methyladenosine32 in tRNA
Identifier
RHEA-COMP:14778
Reactive part
help_outline
- Name help_outline 2'-O-methyladenosine 5'-phosphate residue Identifier CHEBI:74477 Charge -1 Formula C11H13N5O6P Positionhelp_outline 32 SMILEShelp_outline NC1=NC=NC2=C1N=CN2[C@@H]3O[C@H](COP(=O)(*)[O-])[C@@H](O*)[C@H]3OC 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline S-adenosyl-L-homocysteine Identifier CHEBI:57856 Charge 0 Formula C14H20N6O5S InChIKeyhelp_outline ZJUKTBDSGOFHSH-WFMPWKQPSA-N SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](CSCC[C@H]([NH3+])C([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 792 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:56884 | RHEA:56885 | RHEA:56886 | RHEA:56887 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Methylation at position 32 of tRNA catalyzed by TrmJ alters oxidative stress response in Pseudomonas aeruginosa.
Jaroensuk J., Atichartpongkul S., Chionh Y.H., Wong Y.H., Liew C.W., McBee M.E., Thongdee N., Prestwich E.G., DeMott M.S., Mongkolsuk S., Dedon P.C., Lescar J., Fuangthong M.
Bacteria respond to environmental stresses using a variety of signaling and gene expression pathways, with translational mechanisms being the least well understood. Here, we identified a tRNA methyltransferase in Pseudomonas aeruginosa PA14, trmJ, which confers resistance to oxidative stress. Anal ... >> More
Bacteria respond to environmental stresses using a variety of signaling and gene expression pathways, with translational mechanisms being the least well understood. Here, we identified a tRNA methyltransferase in Pseudomonas aeruginosa PA14, trmJ, which confers resistance to oxidative stress. Analysis of tRNA from a trmJ mutant revealed that TrmJ catalyzes formation of Cm, Um, and, unexpectedly, Am. Defined in vitro analyses revealed that tRNA<sup>Met(CAU)</sup> and tRNA<sup>Trp(CCA)</sup> are substrates for Cm formation, tRNA<sup>Gln(UUG)</sup>, tRNA<sup>Pro(UGG)</sup>, tRNA<sup>Pro(CGG)</sup> and tRNA<sup>His(GUG)</sup> for Um, and tRNA<sup>Pro(GGG)</sup> for Am. tRNA<sup>Ser(UGA)</sup>, previously observed as a TrmJ substrate in Escherichia coli, was not modified by PA14 TrmJ. Position 32 was confirmed as the TrmJ target for Am in tRNA<sup>Pro(GGG)</sup> and Um in tRNA<sup>Gln(UUG)</sup> by mass spectrometric analysis. Crystal structures of the free catalytic N-terminal domain of TrmJ show a 2-fold symmetrical dimer with an active site located at the interface between the monomers and a flexible basic loop positioned to bind tRNA, with conformational changes upon binding of the SAM-analog sinefungin. The loss of TrmJ rendered PA14 sensitive to H<sub>2</sub>O<sub>2</sub> exposure, with reduced expression of oxyR-recG, katB-ankB, and katE These results reveal that TrmJ is a tRNA:Cm32/Um32/Am32 methyltransferase involved in translational fidelity and the oxidative stress response. << Less
Nucleic Acids Res. 44:10834-10848(2016) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.