Skip to main content
Kent Academic Repository

Protein transport by the bacterial Tat pathway.

Patel, Roshani, Smith, Sarah M., Robinson, Colin (2014) Protein transport by the bacterial Tat pathway. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1843 (8). pp. 1620-1628. ISSN 0167-4889. (doi:10.1016/j.bbamcr.2014.02.013) (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) (KAR id:42021)

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.
Official URL:
http://dx.doi.org/10.1016/j.bbamcr.2014.02.013

Abstract

The twin-arginine translocation (Tat) system accomplishes the remarkable feat of translocating large – even dimeric – proteins across tightly sealed energy-transducing membranes. All of the available evidence indicates that it is unique in terms of both structure and mechanism; however its very nature has hindered efforts to probe the core translocation events. At the heart of the problem is the fact that two large sub-complexes are believed to coalesce to form the active translocon, and ‘capturing’ this translocation event has been too difficult. Nevertheless, studies on the individual components have come a long way in recent years, and structural studies have reached the point where educated guesses can be made concerning the most interesting aspects of Tat. In this article we review these studies and the emerging ideas in this field. This article is part of a Special Issue entitled: Protein trafficking and secretion in bacteria. Guest Editors: Anastassios Economou and Ross Dalbey.

Item Type: Article
DOI/Identification number: 10.1016/j.bbamcr.2014.02.013
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Susan Davies
Date Deposited: 29 Jul 2014 13:42 UTC
Last Modified: 17 Aug 2022 10:57 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/42021 (The current URI for this page, for reference purposes)

University of Kent Author Information

  • Depositors only (login required):

Total unique views for this document in KAR since July 2020. For more details click on the image.