JCB logo
PeproTech: Cell Culture Supplements
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online
doi:10.1083/jcb.200707196
The Journal of Cell Biology, Vol. 180, No. 6, 1149-1161
The Rockefeller University Press, 0021-9525 $30.00
© Jiang et al.
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 2836K)
Right arrow PPT slides of all figures
Right arrow Supplemental Material Index
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Jiang, Y.
Right arrow Articles by Gilmore, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jiang, Y.
Right arrow Articles by Gilmore, R.
Related Collections
Right arrowRelated In this Issue article
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

Article

An interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation



Ying Jiang, Zhiliang Cheng, Elisabet C. Mandon, and Reid Gilmore

Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605

Correspondence to Reid Gilmore: reid.gilmore{at}umassmed.edu

The signal recognition particle (SRP)–dependent targeting pathway facilitates rapid, efficient delivery of the ribosome–nascent chain complex (RNC) to the protein translocation channel. We test whether the SRP receptor (SR) locates a vacant protein translocation channel by interacting with the yeast Sec61 and Ssh1 translocons. Surprisingly, the slow growth and cotranslational translocation defects caused by deletion of the transmembrane (TM) span of yeast SRβ (SRβ-{Delta}TM) are exaggerated when the SSH1 gene is disrupted. Disruption of the SBH2 gene, which encodes the β subunit of the Ssh1p complex, likewise causes a growth defect when combined with SRβ-{Delta}TM. Cotranslational translocation defects in the ssh1{Delta}SRβ-{Delta}TM mutant are explained by slow and inefficient in vivo gating of translocons by RNCs. A critical function for translocation channel β subunits in the SR–channel interaction is supported by the observation that simultaneous deletion of Sbh1p and Sbh2p causes a defect in the cotranslational targeting pathway that is similar to the translocation defect caused by deletion of either subunit of the SR.

Z. Cheng's present address is Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720.

Abbreviations used in this paper: CPY, carboxypeptidase Y; DPAPB, dipeptidylaminopeptidase B; GEF, guanine nucleotide exchange factor; pDPAPB, DPAPB precursor; RNC, ribosome–nascent chain complex; SR, SRP receptor; SRP, signal recognition particle; TM, transmembrane; Ub, ubiquitin; UTA, Ub translocation assay.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?

Related In this Issue article

The SR finds the translocon
Nicole LeBrasseur
J. Cell Biol. 2008 180: 1053. [Full Text] [PDF]



This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents