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A novel single amino acid change in small subunit ribosomal protein S5 has profound effects on translational fidelity

Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, Iowa 50011, USA

Reprint requests to: Gloria M. Culver, Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA; e-mail: gculver{at}iastate.edu; fax: (515) 294-0453.

S5 is a small subunit ribosomal protein (r-protein) linked to the functional center of the 30S ribosomal subunit. In this study we have identified a unique amino acid mutation in Escherichia coli S5 that produces spectinomycin-resistance and cold sensitivity. This mutation significantly alters cell growth, folding of 16S ribosomal RNA, and translational fidelity. While translation initiation is not affected, both +1 and –1 frameshifting and nonsense suppression are greatly enhanced in the mutant strain. Interestingly, this S5 ribosome ambiguity-like mutation is spatially remote from previously identified S5 ribosome ambiguity (ram) mutations. This suggests that the mechanism responsible for ram phenotypes in the novel mutant strain is possibly distinct from those proposed for other known S5 (and S4) ram mutants. This study highlights the importance of S5 in ribosome function and cell physiology, and suggests that translational fidelity can be regulated in multiple ways.

Keywords: E. coli; 30S ribosome; S5 protein; ram mutant; spectinomycin resistance

¹ These authors contributed equally to this work.

Article published online ahead of print. Article and publication date are at http://www.rnajournal.org/cgi/doi/10.1261/rna.302006.

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