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| | ==Methylation at position 32 of tRNA catalyzed by TrmJ alters oxidative stress response in Pseudomonas aeruiginosa== | | ==Methylation at position 32 of tRNA catalyzed by TrmJ alters oxidative stress response in Pseudomonas aeruiginosa== |
| - | <StructureSection load='5gmc' size='340' side='right' caption='[[5gmc]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='5gmc' size='340' side='right'caption='[[5gmc]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5gmc]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GMC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GMC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5gmc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GMC FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gm8|5gm8]], [[5gmb|5gmb]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">trmJ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5gmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gmc OCA], [https://pdbe.org/5gmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gmc RCSB], [https://www.ebi.ac.uk/pdbsum/5gmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gmc ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/tRNA_(cytidine(32)/uridine(32)-2'-O)-methyltransferase tRNA (cytidine(32)/uridine(32)-2'-O)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.200 2.1.1.200] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5gmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gmc OCA], [http://pdbe.org/5gmc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gmc RCSB], [http://www.ebi.ac.uk/pdbsum/5gmc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gmc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A072ZPM2_PSEAI A0A072ZPM2_PSEAI]] Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.[RuleBase:RU362024] | + | [https://www.uniprot.org/uniprot/A0A072ZPM2_PSEAI A0A072ZPM2_PSEAI] Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.[RuleBase:RU362024] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5gmc" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5gmc" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[TRNA methyltransferase 3D structures|TRNA methyltransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atichartpongkul, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Chionh, Y H]]
| + | |
| - | [[Category: DeMott, M S]]
| + | |
| - | [[Category: Dedon, P C]]
| + | |
| - | [[Category: Fuangthong, M]]
| + | |
| - | [[Category: Jaroensuk, J]]
| + | |
| - | [[Category: Lescar, J]]
| + | |
| - | [[Category: Liew, C W]]
| + | |
| - | [[Category: McBee, M E]]
| + | |
| - | [[Category: Mongkolsuk, S]]
| + | |
| - | [[Category: Prestwich, E G]]
| + | |
| - | [[Category: Thongdee, N]]
| + | |
| - | [[Category: Wong, Y H]]
| + | |
| - | [[Category: Oxidative stress]]
| + | |
| | [[Category: Pseudomonas aeruginosa]] | | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: Transferase]] | + | [[Category: Atichartpongkul S]] |
| - | [[Category: Trmj]] | + | [[Category: Chionh YH]] |
| - | [[Category: Trna methyltransferase]] | + | [[Category: DeMott MS]] |
| - | [[Category: Trna modification]] | + | [[Category: Dedon PC]] |
| - | [[Category: Wobble base]] | + | [[Category: Fuangthong M]] |
| | + | [[Category: Jaroensuk J]] |
| | + | [[Category: Lescar J]] |
| | + | [[Category: Liew CW]] |
| | + | [[Category: McBee ME]] |
| | + | [[Category: Mongkolsuk S]] |
| | + | [[Category: Prestwich EG]] |
| | + | [[Category: Thongdee N]] |
| | + | [[Category: Wong YH]] |
| Structural highlights
Function
A0A072ZPM2_PSEAI Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.[RuleBase:RU362024]
Publication Abstract from PubMed
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(Met(CAU)) and tRNA(Trp(CCA)) are substrates for Cm formation, tRNA(Gln(UUG)), tRNA(Pro(UGG)), tRNA(Pro(CGG)) and tRNA(His(GUG)) for Um, and tRNA(Pro(GGG)) for Am. tRNA(Ser(UGA)), 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(Pro(GGG)) and Um in tRNA(Gln(UUG)) 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 H2O2 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.
Methylation at position 32 of tRNA catalyzed by TrmJ alters oxidative stress response in Pseudomonas aeruginosa.,Jaroensuk J, Atichartpongkul S, Chionh YH, Wong YH, Liew CW, McBee ME, Thongdee N, Prestwich EG, DeMott MS, Mongkolsuk S, Dedon PC, Lescar J, Fuangthong M Nucleic Acids Res. 2016 Dec 15;44(22):10834-10848. doi: 10.1093/nar/gkw870. Epub , 2016 Sep 28. PMID:27683218[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jaroensuk J, Atichartpongkul S, Chionh YH, Wong YH, Liew CW, McBee ME, Thongdee N, Prestwich EG, DeMott MS, Mongkolsuk S, Dedon PC, Lescar J, Fuangthong M. Methylation at position 32 of tRNA catalyzed by TrmJ alters oxidative stress response in Pseudomonas aeruginosa. Nucleic Acids Res. 2016 Dec 15;44(22):10834-10848. doi: 10.1093/nar/gkw870. Epub , 2016 Sep 28. PMID:27683218 doi:http://dx.doi.org/10.1093/nar/gkw870
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