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Transport and proofreading of proteins by the twin-arginine translocation (Tat) system in bacteria

Robinson, Colin, Matos, Cristina F.R.O., Beck, Daniel, Ren, Chao, Lawrence, Janna, Vasisht, Nishi, Mendel, Sharon (2011) Transport and proofreading of proteins by the twin-arginine translocation (Tat) system in bacteria. Biochimica Et Biophysica Acta-Biomembranes, 1808 (3). pp. 876-884. ISSN 0005-2736. (doi:10.1016/j.bbamem.2010.11.023) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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Official URL
http://dx.doi.org/10.1016/j.bbamem.2010.11.023

Abstract

The twin-arginine translocation (Tat) system operates in plant thylakoid membranes and the plasma membranes of most free-living bacteria. In bacteria, it is responsible for the export of a number of proteins to the periplasm, outer membrane or growth medium, selecting substrates by virtue of cleavable N-terminal signal peptides that contain a key twin-arginine motif together with other determinants. Its most notable attribute is its ability to transport large folded proteins (even oligomeric proteins) across the tightly sealed plasma membrane. In Gram-negative bacteria, TatABC subunits appear to carry out all of the essential translocation functions in the form of two distinct complexes at steady state: a TatABC substrate-binding complex and separate TatA complex. Several studies favour a model in which these complexes transiently coalesce to generate the full translocase. Most Gram-positive organisms possess an even simpler “minimalist” Tat system which lacks a TatB component and contains, instead, a bifunctional TatA component. These Tat systems may involve the operation of a TatAC complex together with a separate TatA complex, although a radically different model for TatAC-type systems has also been proposed. While bacterial Tat systems appear to require the presence of only a few proteins for the actual translocation event, there is increasing evidence for the operation of ancillary components that carry out sophisticated “proofreading” activities. These activities ensure that redox proteins are only exported after full assembly of the cofactor, thereby avoiding the futile export of apo-forms. This article is part of a Special Issue entitled Protein translocation across or insertion into membranes.

Item Type: Article
DOI/Identification number: 10.1016/j.bbamem.2010.11.023
Uncontrolled keywords: Tat; Twin-arginine; Protein transport; Signal peptide; Membrane protein
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Colin Robinson
Date Deposited: 24 Jul 2013 15:40 UTC
Last Modified: 29 May 2019 10:26 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/34848 (The current URI for this page, for reference purposes)
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