Molecular Biology of the Cell Call for Nominations: MBC Editor-in-Chief

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
QUICK SEARCH:   [advanced]


     

MBC in Press, published online ahead of print May 16, 2007
Mol. Biol. Cell 10.1091/mbc.E07-02-0117

A more recent version of this article appeared on July 1, 2007
This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
E07-02-0117v1
18/7/2728    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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 Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bradshaw, N.
Right arrow Articles by Walter, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bradshaw, N.
Right arrow Articles by Walter, P.

Submitted on March 1, 2007
Revised on April 25, 2007
Accepted on May 3, 2007

The SRP RNA Links Conformational Changes in the SRP to Protein Targeting

Niels Bradshaw and Peter Walter

Howard Hughes Medical Institute and Department of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, CA 94158

Monitoring Editor: Reid Gilmore

The RNA component of the signal recognition particle (SRP) is universally required for cotranslational protein targeting. Biochemical studies have shown that SRP RNA participates in the central step of protein targeting by catalyzing the interaction of the SRP with the SRP receptor (SR). SRP RNA also accelerates GTP hydrolysis in the SRP•SR complex once formed. Using a reverse-genetic and biochemical analysis, we identified mutations in the E. coli SRP protein, Ffh, that abrogate the activity of the SRP RNA and cause corresponding targeting defects in vivo. The mutations in Ffh that disrupt SRP RNA activity map to regions that undergo dramatic conformational changes during the targeting reaction, suggesting that the activity of the SRP RNA is linked to the major conformational changes in the signal sequence binding subunit of the SRP. In this way, the SRP RNA may coordinate the interaction of the SRP and the SR with ribosome recruitment and transfer to the translocon, explaining why the SRP RNA is an indispensable component of the protein targeting machinery.

Address correspondence to: Peter Walter (pwalter{at}biochem.ucsf.edu)




This article has been cited by other articles:


Home page
 Proc. Natl. Acad. Sci. USAHome page
T. Hainzl, S. Huang, and A. E. Sauer-Eriksson
Interaction of signal-recognition particle 54 GTPase domain and signal-recognition particle RNA in the free signal-recognition particle
PNAS, September 18, 2007; 104(38): 14911 - 14916.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2007 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.