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Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY

Cannon, Kurt S. and Or, Eran and Clemons, William M., Jr. and Shibata, Yoko and Rapoport, Tom A. (2005) Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY. Journal of Cell Biology, 169 (2). pp. 219-225. ISSN 0021-9525. PMCID PMC2171872. http://resolver.caltech.edu/CaltechAUTHORS:20181029-143602744

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Abstract

During their biosynthesis, many proteins pass through the membrane via a hydrophilic channel formed by the heterotrimeric Sec61/SecY complex. Whether this channel forms at the interface of multiple copies of Sec61/SecY or is intrinsic to a monomeric complex, as suggested by the recently solved X-ray structure of the Methanococcus jannaschii SecY complex, is a matter of contention. By introducing a single cysteine at various positions in Escherichia coli SecY and testing its ability to form a disulfide bond with a single cysteine in a translocating chain, we provide evidence that translocating polypeptides pass through the center of the SecY complex. The strongest cross-links were observed with residues that would form a constriction in an hourglass-shaped pore. This suggests that the channel makes only limited contact with a translocating polypeptide, thus minimizing the energy required for translocation.


Item Type:Article
Related URLs:
URLURL TypeDescription
https://doi.org/10.1083/jcb.200412019DOIArticle
http://www.jcb.org/cgi/content/full/jcb.200412019/DC1PublisherSupplemental Material
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171872PubMed CentralArticle
ORCID:
AuthorORCID
Clemons, William M., Jr.0000-0002-0021-889X
Additional Information:© 2005 Rockefeller University Press. After the Initial Publication Period, RUP will grant to the public the non-exclusive right to copy, distribute, or display the Article under a Creative Commons Attribution-Noncommercial-Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode, or updates thereof. Submitted: 2 December 2004; Accepted: 4 March 2005. Thanks to Drs. Wendy Garrett, Tommy Kirchhausen, Andrew Osborne, and Pamela Wearsch for critical reading of the manuscript. We thank Andrew Osborne (T. Rapoport's laboratory) for the cysteine-free SecA mutant. This work was supported by a National Institutes of Health grant to T.A. Rapoport. K.S. Cannon is a Richard D. Frisbee III Foundation Fellow of the Leukemia & Lymphoma Society. W.M. Clemons Jr. has a fellowship from the Damon Runyon Cancer Research Foundation. T.A. Rapoport is a Howard Hughes Medical Institute Investigator.
Funders:
Funding AgencyGrant Number
NIHUNSPECIFIED
Leukemia and Lymphoma SocietyUNSPECIFIED
Damon Runyon Cancer Research FoundationUNSPECIFIED
Howard Hughes Medical Institute (HHMI)UNSPECIFIED
PubMed Central ID:PMC2171872
Record Number:CaltechAUTHORS:20181029-143602744
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20181029-143602744
Official Citation:Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY. Kurt S. Cannon, Eran Or, William M. Clemons, Yoko Shibata, Tom A. Rapoport. The Journal of Cell Biology Apr 2005, 169 (2) 219-225; DOI: 10.1083/jcb.200412019
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:90475
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:30 Oct 2018 01:47
Last Modified:30 Oct 2018 01:47

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