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Published online ahead of print on 21 April 2009 as doi:10.1099/mic.0.027987-0
Microbiology 2009;155:1776.

Microbiology (2009), DOI 10.1099/mic.0.027987-0
© 2009 Society for General Microbiology
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Microbiology 0 (2009), mic.0.027987; DOI  10.1099/mic.0.027987-0
© 2009 Society for General Microbiology

Effects of altered TatC proteins on protein secretion efficiency via the twin-arginine translocation pathway of Bacillus subtilis

R. T. Eijlander1, M. A. Kolbusz1, E. M. Berendsen1 and O. P. Kuipers2,3

1 University of Groningen;
2 University of Groningen, Molecular Genetics

ABSTRACT

Protein translocation via the Tat machinery in thylakoids and bacteria occurs through a cooperation between the TatA, TatB and TatC subunits, of which the TatC protein forms the initial Tat substrate binding site. The Bacillus subtilis Tat machinery lacks TatB and comprises two separate TatAC complexes with distinct substrate specificities: PhoD is secreted by the TatAdCd complex, whereas YwbN is secreted by the TatAyCy complex. To study the role of the Gram-positive TatC proteins on Tat-dependent protein secretion efficiency, we applied several genetic engineering approaches to modify and analyse the B. subtilis TatCd and TatCy proteins. Cytoplasmic and transmembrane domain exchange between TatCd and TatCy resulted in stable chimeric proteins that were unable to secrete both known substrates of B. subtilis. Site-directed mutagenesis of conserved residues in the N-terminal part of both TatC proteins revealed significant differences in the degree of importance of these residues between TatCd, TatCy and E. coli TatC. In addition, two small C-terminal deletions in TatCy resulted in complete abolishment of YwbN translocation, indicating that this terminus is essential for Tat translocation activity. Important differences with previous observations for E. coli TatC and implications for substrate binding and translocation are discussed.

3 E-mail: o.p.kuipers{at}rug.nl






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Copyright © 2009 Society for General Microbiology.