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Shoji, S, Janssen, BD, Hayes, CS and Fredrick, K (2010) Translation factor LepA contributes to tellurite resistance in Escherichia coli but plays no apparent role in the fidelity of protein synthesis. Biochimie 92:157-63


LepA is a translational GTPase highly conserved in bacterial lineages. While it has been shown that LepA can catalyze reverse ribosomal translocation in vitro, the role of LepA in the cell remains unclear. Here, we show that deletion of the lepA gene (DeltalepA) in Escherichia coli causes hypersensitivity to potassium tellurite and penicillin G, but has no appreciable effect on growth under many other conditions. DeltalepA does not increase miscoding or frameshifting errors under normal or stress conditions, indicating that LepA does not contribute to the fidelity of translation. Overexpression of LepA interferes with tmRNA-mediated peptide tagging and A-site mRNA cleavage, suggesting that LepA is a bona fide translation factor that can act on stalled ribosomes with a vacant A site in vivo. Together these results lead us to hypothesize that LepA is involved in co-translational folding of proteins that are otherwise vulnerable to tellurite oxidation.


PubMed PMC2815024 Online version:10.1016/j.biochi.2009.11.002


Drug Resistance, Bacterial; Escherichia coli/cytology; Escherichia coli/drug effects; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/biosynthesis; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; GTP Phosphohydrolases/deficiency; GTP Phosphohydrolases/genetics; Gene Deletion; Oxidants/pharmacology; Phosphoproteins/deficiency; Phosphoproteins/genetics; Protein Biosynthesis/physiology; RNA, Messenger/genetics; Tellurium/pharmacology; Transcriptional Elongation Factors/deficiency; Transcriptional Elongation Factors/genetics; Transcriptional Elongation Factors/metabolism


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