TRNA methyltransferase

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Revision as of 07:46, 20 August 2024

spinqualitylabelsall models Structure of tRNA methyltransferase for N1 of guanine 37 complex with S-adenosylhomocysteine (PDB entry 1uak) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function tRNA methyltransferase (Trm) methylates specific positions on tRNA. tRNA methylation is a post-transcription modification. The methyl donor is S-adenosylmethionine (SAM) and the product is the methylated tRNA and S-adenosylhomocysteine (SAH)[1]. S-adenosylornithine or sinefugin (SFG) is an inhibitor of the reaction. For details on Trm to N2 of guanine 6 see TRNA:m2G6 methyltransferase TrmN/Trm14. Dual specificity tRNA methyltransferase Rlmn is an E. coli methyltransferase which modifies both ribosomal 23S RNA and tRNA[2]. Structural highlights Trm is located at the cleft at the subunit interface[3]. Water molecules are shown as red spheres. 3D structures of tRNA methyltransferase tRNA methyltransferase 3D structures

References

1. ↑ Swinehart WE, Jackman JE. Diversity in mechanism and function of tRNA methyltransferases. RNA Biol. 2015;12(4):398-411. doi: 10.1080/15476286.2015.1008358. PMID:25626150 doi:http://dx.doi.org/10.1080/15476286.2015.1008358
2. ↑ Benitez-Paez A, Villarroya M, Armengod ME. The Escherichia coli RlmN methyltransferase is a dual-specificity enzyme that modifies both rRNA and tRNA and controls translational accuracy. RNA. 2012 Oct;18(10):1783-95. doi: 10.1261/rna.033266.112. Epub 2012 Aug 13. PMID:22891362 doi:http://dx.doi.org/10.1261/rna.033266.112
3. ↑ Ahn HJ, Kim HW, Yoon HJ, Lee BI, Suh SW, Yang JK. Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognition. EMBO J. 2003 Jun 2;22(11):2593-603. PMID:12773376 doi:10.1093/emboj/cdg269