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The twin arginine protein transport (Tat) system transports folded proteins across cytoplasmic membranes of bacteria and thylakoid membranes of plants, and in Escherichia coli it comprises TatA, TatB and TatC components. In this study we show that the membrane extrinsic domain of TatB forms parallel contacts with at least one other TatB protein. Truncation of the C-terminal two thirds of TatB still allows complex formation with TatC, although protein transport is severely compromised. We were unable to isolate transport-inactive single codon substitution mutations in tatB suggesting that the precise amino acid sequence of TatB is not critical to its function. Structured summary: TatA physically interacts with TatA by two hybrid (View interaction) TatB and TatC bind by molecular sieving (View interaction) TatB physically interacts with TatB by two hybrid (View Interaction 1, 2) © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Original publication

DOI

10.1016/j.febslet.2011.01.016

Type

Journal article

Journal

FEBS Letters

Publication Date

04/02/2011

Volume

585

Pages

478 - 484