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Contributions of the Transmembrane Domain and a Key Acidic Motif to Assembly and Function of the TatA Complex

Warren, Gemma, Oates, Joanne, Robinson, Colin, Dixon, Ann M. (2009) Contributions of the Transmembrane Domain and a Key Acidic Motif to Assembly and Function of the TatA Complex. Journal of Molecular Biology, 388 (1). pp. 122-132. ISSN 0022-2836. (doi:10.1016/j.jmb.2009.02.060) (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)

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. (Contact us about this Publication)
Official URL
http://dx.doi.org/10.1016/j.jmb.2009.02.060

Abstract

The twin-arginine translocase (Tat) pathway transports folded proteins across bacterial and thylakoid membranes. In Escherichia coli, a membrane-bound TatA complex, which oligomerizes to form complexes of less than 100 to more than 500 kDa, is considered essential for translocation. We have studied the contributions of various TatA domains to the assembly and function of this heterogeneous TatA complex. The TOXCAT assay was used to analyze the potential contribution of the TatA transmembrane (TM) domain. We observed relatively weak interactions between TatA TM domains, suggesting that the TM domain is not the sole driving force behind oligomerization. A potential hydrogen-bonding role for a TM domain glutamine was also investigated, and it was found that mutation blocks transport at low expression levels, while assembly is unaffected at higher expression levels. Analysis of truncated TatA proteins instead highlighted an acidic motif directly following the TatA amphipathic helix. Mutating these negatively charged residues to apolar uncharged residues completely blocks activity, even at high levels of TatA, and appears to disrupt ordered complex formation.

Item Type: Article
DOI/Identification number: 10.1016/j.jmb.2009.02.060
Uncontrolled keywords: protein transport; twin-arginine translocase; TatA; transmembrane domain; TOXCAT
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Colin Robinson
Date Deposited: 24 Jul 2013 15:43 UTC
Last Modified: 29 May 2019 10:26 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/34851 (The current URI for this page, for reference purposes)
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