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Nucleic Acids Research Advance Access originally published online on September 29, 2008
Nucleic Acids Research 2008 36(19):6187-6198; doi:10.1093/nar/gkn643
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Nucleic Acids Research, 2008, Vol. 36, No. 19 6187-6198
© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Structural Biology

Yeast ribosomal protein L10 helps coordinate tRNA movement through the large subunit

Alexey N. Petrov, Arturas Meskauskas, Sara C. Roshwalb and Jonathan D. Dinman*

Department of Cell Biology and Molecular Genetics, University of Maryland, 2135 Microbiology Building, College Park, MD 20742, USA

*To whom correspondence should be addressed. Tel: +1 301 405 0918; Fax: +1 301 314 9489; Email: dinman{at}umd.edu

Received August 4, 2008. Revised September 16, 2008. Accepted September 17, 2008.

Yeast ribosomal protein L10 (E. coli L16) is located at the center of a topological nexus that connects many functional regions of the large subunit. This essential protein has previously been implicated in processes as diverse as ribosome biogenesis, translational fidelity and mRNA stability. Here, the inability to maintain the yeast Killer virus was used as a proxy for large subunit defects to identify a series of L10 mutants. These mapped to roughly four discrete regions of the protein. A detailed analysis of mutants located in the N-terminal ‘hook’ of L10, which inserts into the bulge of 25S rRNA helix 89, revealed strong effects on rRNA structure corresponding to the entire path taken by the tRNA 3' end as it moves through the large subunit during the elongation cycle. The mutant-induced structural changes are wide-ranging, affecting ribosome biogenesis, elongation factor binding, drug resistance/hypersensitivity, translational fidelity and virus maintenance. The importance of L10 as a potential transducer of information through the ribosome, and of a possible role of its N-terminal domain in switching between the pre- and post-translocational states are discussed.

Present addresses: Alexey N. Petrov, Department of Structural Biology, Stanford University School of Medicine. D105 Fairchild Science Building, 299 Campus Drive West, Stanford, CA 94305-5126, USA Sara C. Roshwalb, University of Tennessee College of Veterinary Medicine. 2407 River Dr Knoxville, TN 37996, USA


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