Skip Navigation



Nucleic Acids Research Advance Access published online on February 7, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn034
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (6003K) Freely available
Right arrow Screen PDF (1121K) Freely available
Right arrow Supplementary Data
Right arrowOA All Versions of this Article:
36/6/1826    most recent
gkn034v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Meskauskas, A.
Right arrow Articles by Dinman, J. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Meskauskas, A.
Right arrow Articles by Dinman, J. D.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 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

Structure/function analysis of yeast ribosomal protein L2

Arturas Meskauskas, Johnathan R. Russ and Jonathan D. Dinman*

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: +(301) 405 0918; Fax: +(301) 314 9489; Email: dinman{at}umd.edu

Received December 7, 2007. Revised January 18, 2008. Accepted January 21, 2008.

Ribosomal protein L2 is a core element of the large subunit that is highly conserved among all three kingdoms. L2 contacts almost every domain of the large subunit rRNA and participates in an intersubunit bridge with the small subunit rRNA. It contains a solvent-accessible globular domain that interfaces with the solvent accessible side of the large subunit that is linked through a bridge to an extension domain that approaches the peptidyltransferase center. Here, screening of randomly generated library of yeast RPL2A alleles identified three translationally defective mutants, which could be grouped into two classes. The V48D and L125Q mutants map to the globular domain. They strongly affect ribosomal A-site associated functions, peptidyltransferase activity and subunit joining. H215Y, located at the tip of the extended domain interacts with Helix 93. This mutant specifically affects peptidyl–tRNA binding and peptidyltransferase activity. Both classes affect rRNA structure far away from the protein in the A-site of the peptidyltransferase center. These findings suggest that defective interactions with Helix 55 and with the Helix 65–66 structure may indicate a certain degree of flexibility in L2 in the neck region between the two other domains, and that this might help to coordinate tRNA–ribosome interactions.

Present address: Johnathan R. Russ, The University of Chicago Press, Journals Division, 1427 East 60th Street, Chicago, IL 60637, USA The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
J. D. Dinman
The Eukaryotic Ribosome: Current Status and Challenges
J. Biol. Chem., May 1, 2009; 284(18): 11761 - 11765.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
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]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.