Nucleic Acids Research Advance Access originally published online on January 18, 2008
Nucleic Acids Research 2008 36(5):1497-1507; doi:10.1093/nar/gkm1179
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Nucleic Acids Research, 2008, Vol. 36, No. 5 1497-1507
© 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.
RNA |
rRNA mutants in the yeast peptidyltransferase center reveal allosteric information networks and mechanisms of drug resistance
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 November 27, 2007. Revised December 24, 2007. Accepted December 26, 2007.
To ensure accurate and rapid protein synthesis, nearby and distantly located functional regions of the ribosome must dynamically communicate and coordinate with one another through a series of information exchange networks. The ribosome is 
2/3 rRNA and information should pass mostly through this medium. Here, two viable mutants located in the peptidyltransferase center (PTC) of yeast ribosomes were created using a yeast genetic system that enables stable production of ribosomes containing only mutant rRNAs. The specific mutants were C2820U (Escherichia coli C2452) and 
2922C (E. coli U2554). Biochemical and genetic analyses of these mutants suggest that they may trap the PTC in the ‘open’ or aa-tRNA bound conformation, decreasing peptidyl-tRNA binding. We suggest that these structural changes are manifested at the biological level by affecting large ribosomal subunit biogenesis, ribosomal subunit joining during initiation, susceptibility/resistance to peptidyltransferase inhibitors, and the ability of ribosomes to properly decode termination codons. These studies also add to our understanding of how information is transmitted both locally and over long distances through allosteric networks of rRNA–rRNA and rRNA–protein interactions.
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  N. Van Dyke, B. F. Pickering, and M. W. Van Dyke Stm1p alters the ribosome association of eukaryotic elongation factor 3 and affects translation elongation Nucleic Acids Res., October 1, 2009; 37(18): 6116 - 6125. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. D. Dinman The Eukaryotic Ribosome: Current Status and Challenges J. Biol. Chem., May 1, 2009; 284(18): 11761 - 11765. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K. Fujii, M. Kitabatake, T. Sakata, A. Miyata, and M. Ohno A role for ubiquitin in the clearance of nonfunctional rRNAs Genes & Dev., April 15, 2009; 23(8): 963 - 974. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. N. Petrov, A. Meskauskas, S. C. Roshwalb, and J. D. Dinman Yeast ribosomal protein L10 helps coordinate tRNA movement through the large subunit Nucleic Acids Res., November 1, 2008; 36(19): 6187 - 6198. [Abstract] [Full Text] [PDF]
|
|