The bacterial Sec-translocase: structure and mechanism-Reference-Cited by-同舟云学术

The bacterial Sec-translocase: structure and mechanism

Published:2012-04-19 Issue:1592 Volume:367 Page:1016-1028
ISSN:0962-8436
Container-title:Philosophical Transactions of the Royal Society B: Biological Sciences
language:en
Short-container-title:Phil. Trans. R. Soc. B

Author:

Lycklama a Nijeholt Jelger A.¹,Driessen Arnold J. M.¹

Affiliation:

1. Department of Molecular Microbiology, Groningen Biomolecular Science and Biotechnology Institute, and the Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 7, Groningen 9747 AG, The Netherlands

Abstract

Most bacterial secretory proteins pass across the cytoplasmic membrane via the translocase, which consists of a protein-conducting channel SecYEG and an ATP-dependent motor protein SecA. The ancillary SecDF membrane protein complex promotes the final stages of translocation. Recent years have seen a major advance in our understanding of the structural and biochemical basis of protein translocation, and this has led to a detailed model of the translocation mechanism.

Publisher

The Royal Society

Subject

General Agricultural and Biological Sciences,General Biochemistry, Genetics and Molecular Biology

Link

https://royalsocietypublishing.org/doi/pdf/10.1098/rstb.2011.0201

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