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J Biol Chem. 2011 Dec 23;286(51):43679-89. doi: 10.1074/jbc.M111.292565. Epub 2011 Oct 31.

Early contacts between substrate proteins and TatA translocase component in twin-arginine translocation.

Author information

1
Institute of Biochemistry and Molecular Biology, Zentrum für Biochemie und Molekulare Zellforschung (ZBMZ), Faculty of Biology, University of Freiburg, Freiburg, Germany.

Abstract

Twin-arginine translocation (Tat) is a unique protein transport pathway in bacteria, archaea, and plastids. It mediates the transmembrane transport of fully folded proteins, which harbor a consensus twin-arginine motif in their signal sequences. In Gram-negative bacteria and plant chloroplasts, three membrane proteins, named TatA, TatB, and TatC, are required to enable Tat translocation. Available data suggest that TatA assembles into oligomeric pore-like structures that might function as the protein conduit across the lipid bilayer. Using site-specific photo-cross-linking, we have investigated the molecular environment of TatA under resting and translocating conditions. We find that monomeric TatA is an early interacting partner of functionally targeted Tat substrates. This interaction with TatA likely precedes translocation of Tat substrates and is influenced by the proton-motive force. It strictly depends on the presence of TatB and TatC, the latter of which is shown to make contacts with the transmembrane helix of TatA.

PMID:
22041896
PMCID:
PMC3243508
DOI:
10.1074/jbc.M111.292565
[Indexed for MEDLINE]
Free PMC Article

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