The twin-arginine translocation (Tat) systems from Bacillus subtilis display a conserved mode of complex organization and similar substrate recognition requirements

Barnett, James P. and van der Ploeg, René and Eijlander, Robyn T. and Nenninger, Anja and Mendel, Sharon and Rozeboom, Rense and Kuipers, Oscar P. and van Dijl, Jan Maarten and Robinson, Colin (2009) The twin-arginine translocation (Tat) systems from Bacillus subtilis display a conserved mode of complex organization and similar substrate recognition requirements. FEBS Journal, 276 (1). pp. 232-243. ISSN 1742464X. (doi:https://doi.org/10.1111/j.1742-4658.2008.06776.x) (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/10.1111/j.1742-4658.2008.06776.x

Abstract

The twin arginine translocation (Tat) system transports folded proteins across the bacterial plasma membrane. In Gram-negative bacteria, membrane-bound TatABC subunits are all essential for activity, whereas Gram-positive bacteria usually contain only TatAC subunits. In Bacillus subtilis, two TatAC-type systems, TatAdCd and TatAyCy, operate in parallel with different substrate specificities. Here, we show that they recognize similar signal peptide determinants. Both systems translocate green fluorescent protein fused to three distinct Escherichia coli Tat signal peptides, namely DmsA, AmiA and MdoD, and mutagenesis of the DmsA signal peptide confirmed that both Tat pathways recognize similar targeting determinants within Tat signals. Although another E. coli Tat substrate, trimethylamine N-oxide reductase, was translocated by TatAdCd but not by TatAyCy, we conclude that these systems are not predisposed to recognize only specific Tat signal peptides, as suggested by their narrow substrate specificities in B. subtilis. We also analysed complexes involved in the second Tat pathway in B. subtilis, TatAyCy. This revealed a discrete TatAyCy complex together with a separate, homogeneous, ∼ 200 kDa TatAy complex. The latter complex differs significantly from the corresponding E. coli TatA complexes, pointing to major structural differences between Tat complexes from Gram-negative and Gram-positive organisms. Like TatAd, TatAy is also detectable in the form of massive cytosolic complexes.

Item Type: Article
Uncontrolled keywords: Bacillus subtilis;Gram-positive;green fluorescent protein;signal peptide;twin arginine translocation
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Colin Robinson
Date Deposited: 24 Jul 2013 15:47 UTC
Last Modified: 28 Aug 2013 08:30 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/34854 (The current URI for this page, for reference purposes)
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