Nucleic Acids Research Advance Access originally published online on October 2, 2008
Nucleic Acids Research 2008 36(19):6175-6186; doi:10.1093/nar/gkn642
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Nucleic Acids Research, 2008, Vol. 36, No. 19 6175-6186
© 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 |
Ribosomal protein L3 functions as a ‘rocker switch’ to aid in coordinating of large subunit-associated functions in eukaryotes and Archaea
Department of Cell Biology and Molecular Genetics, Microbiology Building Rm. 2135, University of Maryland, College Park, MD 20742, USA
*To whom correspondence should be addressed. Tel: +1 301 405 6030; Fax: +1 301 314 9498; Email: artmeska{at}umd.edu
Correspondence may also be addressed to Jonathan Dinman. Tel: +1 301 405 0918; Fax: +1 301 314 9498; Email: dinman{at}umd.edu
Received August 4, 2008. Revised September 16, 2008. Accepted September 17, 2008.
Although ribosomal RNAs (rRNAs) comprise the bulk of the ribosome and carry out its main functions, ribosomal proteins also appear to play important structural and functional roles. Many ribosomal proteins contain long, nonglobular domains that extend deep into the rRNA cores. In eukaryotes and Archaea, ribosomal protein L3 contains two such extended domains tethered to a common globular hub, thus providing an excellent model to address basic questions relating to ribosomal protein structure/function relationships. Previous work in our laboratory identified the central ‘W-finger’ extension of yeast L3 in helping to coordinate ribosomal functions. New studies on the ‘N-terminal’ extension in yeast suggest that it works with the W-finger to coordinate opening and closing of the corridor through which the 3' end of aa-tRNA moves during the process of accommodation. Additionally, the effect of one of the L3 N-terminal extension mutants on the interaction between C75 of the aa-tRNA and G2921 (Escherichia coli G2553) of 25S rRNA provides the first evidence of the effect of a ribosomal protein on aa-tRNA positioning and peptidyltransfer, possibly through the induced fit model. A model is presented describing how all three domains of L3 may function together as a ‘rocker switch’ to coordinate the stepwise processes of translation elongation.
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