Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1758, Issue 4, Pages 443-451Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2006.03.018
Keywords
protein export; twin-arginine translocation; Bacillus subtilis; complex formation; TatA
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The twin arginine translocation (Tat) system has the capacity to transfer completely folded proteins across the bacterial cytoplasmic membrane and the thylakoid membrane of plant chloroplasts. The most abundant TatA protein of this system has been suggested to form the protein conducting channel. Here, the molecular organisation of soluble and membrane embedded Bacillils subtilis TatA(d) was analysed using negative contrast and freeze-fractured electron microscopy. In both compartments. the protein showed homo-oligomerisation. In aqueous solution, TatAd formed homo-multimeric micelle-like complexes. Freeze-fracture analysis of proteoliposomes revealed self association of membrane-integrated TatAd independent from TatC(d), the second component of this transport system. Immunogold labelling demonstrated that the Substrate prePhoD was co-localised with membrane-integrated TatA(d) complexes. (c) 2006 Elsevier B.V. All rights reserved.
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