Kapoor, S and Samhita, L and Varshney, U (2011) Functional Significance of an Evolutionarily Conserved Alanine (GCA) Resume Codon in tmRNA in Escherichia coli. In: Journal of Bacteriology, 193 (14). pp. 3569-3576. ISSN 0021-9193
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Abstract
Occasionally, ribosomes stall on mRNAs prior to the completion of the polypeptide chain. In Escherichia coli and other eubacteria, tmRNA-mediated trans-translation is a major mechanism that recycles the stalled ribosomes. The tmRNA possesses a tRNA-like domain and a short mRNA region encoding a short peptide (ANDENYALAA in E. coli) followed by a termination codon. The first amino acid (Ala) of this peptide encoded by the resume codon (GCN) is highly conserved in tmRNAs in different species. However, reasons for the high evolutionary conservation of the resume codon identity have remained unclear. In this study, we show that changing the E. coli tmRNA resume codon to other efficiently translatable codons retains efficient functioning of the tmRNA. However, when the resume codon was replaced with the low-usage codons, its function was adversely affected. Interestingly, expression of tRNAs decoding the low-usage codon from plasmid-borne gene copies restored efficient utilization of tmRNA. We discuss why in E. coli, the GCA (Ala) is one of the best codons and why all codons in the short mRNA of the tmRNA are decoded by the abundant tRNAs. © 2011, American Society for Microbiology.
Item Type: | Journal Article |
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Publication: | Journal of Bacteriology |
Publisher: | American Society of Microbiology |
Additional Information: | Copyright for this article belongs to the Author. |
Department/Centre: | Division of Biological Sciences > Microbiology & Cell Biology |
Date Deposited: | 31 Aug 2019 16:18 |
Last Modified: | 01 Jun 2022 10:07 |
URI: | https://eprints.iisc.ac.in/id/eprint/63542 |
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