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Title: | Methylation at position 32 of tRNA catalyzed by TrmJ alters oxidative stress response in Pseudomonas aeruginosa |
Authors: | Juthamas Jaroensuk Sopapan Atichartpongkul Yok Hian Chionh Yee Hwa Wong Chong Wai Liew Megan E. McBee Narumon Thongdee Erin G. Prestwich Michael S. DeMott Skorn Mongkolsuk Peter C. Dedon Julien Lescar Mayuree Fuangthong Chulabhorn Graduate Institute Singapore-MIT Alliance Chulabhorn Research Institute Nanyang Technological University Massachusetts Institute of Technology Mahidol University Center of Excellence on Environmental Health and Toxicology (EHT) Sorbonne Universite Tychan Private Ltd |
Keywords: | Biochemistry, Genetics and Molecular Biology |
Issue Date: | 1-Dec-2016 |
Citation: | Nucleic Acids Research. Vol.44, No.22 (2016), 10834-10848 |
Abstract: | © The Author(s) 2016. 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 tRNAMet(CAU) and tRNATrp(CCA) are substrates for Cm formation, tRNAGln(UUG), tRNAPro(UGG), tRNAPro(CGG) and tRNAHis(GUG) for Um, and tRNAPro(GGG) for Am. tRNASer(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 tRNAPro(GGG) and Um in tRNAGln(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. |
URI: | https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85012254246&origin=inward http://repository.li.mahidol.ac.th/dspace/handle/123456789/42314 |
ISSN: | 13624962 03051048 |
Appears in Collections: | Scopus 2016-2017 |
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