Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (564K) Freely available
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 ISI Web of Science
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 Search for citing articles in:
ISI Web of Science (8)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Venkatesan, A.
Right arrow Articles by Dasgupta, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Venkatesan, A.
Right arrow Articles by Dasgupta, A.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, Vol 27, Issue 2 562-572, Copyright © 1999 by Oxford University Press

ARTICLES

Structure and function of a small RNA that selectively inhibits internal ribosome entry site-mediated translation

A Venkatesan, S Das and A Dasgupta
Molecular Biology Institute, University of California, Los Angeles, CA 90095-1747, USA and Department of Microbiology, Molecular Genetics and Immunology, UCLA School of Medicine, Los Angeles, CA 90095-1747, USA.

A 60 nt long RNA termed IRNA, isolated from the yeast Saccharomyces cerevesiae, was previously shown to selectively block internal ribosome entry site (IRES)-mediated translation without interfering with cap- dependent translation of cellular mRNAs both in vivo and in vitro. IRNA specifically bound cellular proteins believed to be important for IRES- mediated translation. We demonstrate here that a complementary copy of IRNA (cIRNA) is also active in blocking IRES-mediated translation and that it binds many of the same cellular proteins that IRNA does. We have probed the secondary structure of both IRNA and cIRNA using single- strand- and double-strand-specific nucleases as well as using oligonucleotide hybridization followed by RNase H digestion. Both IRNA and cIRNA share secondary structural homology, although distinct differences do exist between the two structures. Mutational analysis of IRNA shows that sequences that form both the main stem and one loop are critical for its translation inhibitory activity. Maintenance of the established secondary structure appears to be required for both IRNA's ability to bind cellular trans -acting proteins believed to be required for IRES-mediated translation and its ability to block IRES-mediated translation.
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. Gen. Virol.Home page
E. Martínez-Salas, R. Ramos, E. Lafuente, and S. López de Quinto
Functional interactions in internal translation initiation directed by viral and cellular IRES elements
J. Gen. Virol., May 1, 2001; 82(5): 973 - 984.
[Full Text]

Home page
 Mol. Cell. Biol.Home page
A. Venkatesan and A. Dasgupta
Novel Fluorescence-Based Screen To Identify Small Synthetic Internal Ribosome Entry Site Elements
Mol. Cell. Biol., April 15, 2001; 21(8): 2826 - 2837.
[Abstract] [Full Text]

Home page
 J. Virol.Home page
C. B. Buck, X. Shen, M. A. Egan, T. C. Pierson, C. M. Walker, and R. F. Siliciano
The Human Immunodeficiency Virus Type 1 gag Gene Encodes an Internal Ribosome Entry Site
J. Virol., January 1, 2001; 75(1): 181 - 191.
[Abstract] [Full Text]

Home page
 Microbiol. Mol. Biol. Rev.Home page
M. Gale Jr., S.-L. Tan, and M. G. Katze
Translational Control of Viral Gene Expression in Eukaryotes
Microbiol. Mol. Biol. Rev., June 1, 2000; 64(2): 239 - 280.
[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.