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Salt Sensitivity of Minimal Twin Arginine Translocases

van der Ploeg, René, Barnett, James P., Vasisht, Nishi, Goosens, Vivianne J., Pother, Dierk C., Robinson, Colin, van Dijl, Jan Maarten (2011) Salt Sensitivity of Minimal Twin Arginine Translocases. Journal of Biological Chemistry, 286 (51). pp. 43759-43770. ISSN 0021-9258. (doi:10.1074/jbc.M111.243824) (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/10.1074/jbc.M111.243824

Abstract

Bacterial twin arginine translocation (Tat) pathways have evolved to facilitate transport of folded proteins across membranes. Gram-negative bacteria contain a TatABC translocase composed of three subunits named TatA, TatB, and TatC. In contrast, the Tat translocases of most Gram-positive bacteria consist of only TatA and TatC subunits. In these minimal TatAC translocases, a bifunctional TatA subunit fulfils the roles of both TatA and TatB. Here we have probed the importance of conserved residues in the bifunctional TatAy subunit of Bacillus subtilis by site-specific mutagenesis. A set of engineered TatAy proteins with mutations in the cytoplasmic hinge and amphipathic helix regions were found to be inactive in protein translocation under standard growth conditions for B. subtilis or when heterologously expressed in Escherichia coli. Nevertheless, these mutated TatAy proteins did assemble into TatAy and TatAyCy complexes, and they facilitated membrane association of twin arginine precursor proteins in E. coli. Interestingly, most of the mutated TatAyCy translocases were salt-sensitive in B. subtilis. Similarly, the TatAC translocases of Bacillus cereus and Staphylococcus aureus were salt-sensitive when expressed in B. subtilis. Taken together, our present observations imply that salt-sensitive electrostatic interactions have critical roles in the preprotein translocation activity of certain TatAC type translocases from Gram-positive bacteria.

Item Type: Article
DOI/Identification number: 10.1074/jbc.M111.243824
Uncontrolled keywords: Bacteria Protein Secretion Protein Translocation Secretion Sorting Bacillus Listeria Staphylococcus YwbN Twin Arginine
Subjects: Q Science
Q Science > QH Natural history > QH301 Biology
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Colin Robinson
Date Deposited: 03 Oct 2013 09:07 UTC
Last Modified: 29 May 2019 11:05 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/35364 (The current URI for this page, for reference purposes)
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