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J Biol Chem, Vol. 273, Issue 29, 18003-18006, July 17, 1998
From the Proteins are transported across the bacterial
plasma membrane and the chloroplast thylakoid membrane by means of
protein translocases that recognize N-terminal targeting signals in
their cognate substrates. Transport of many of these proteins involves
the well defined Sec apparatus that operates in both membranes. We
describe here the identification of a novel component of a bacterial
Sec-independent translocase. The system probably functions in a similar
manner to a Sec-independent translocase in the thylakoid membrane, and substrates for both systems bear a characteristic twin-arginine motif
in the targeting peptide. The translocase component is encoded in
Escherichia coli by an unassigned reading frame,
yigU, disruption of which blocks the export of at least
five twin-Arg-containing precursor proteins that are predicted to bind
redox cofactors, and hence fold, prior to translocation. The Sec
pathway remains unaffected in the deletion strain. The gene has been
designated tatC (for twin-arginine
translocation), and we show that homologous genes are
present in a range of bacteria, plastids, and mitochondria. These
findings suggest a central role for TatC-type proteins in the
translocation of tightly folded proteins across a spectrum of
biological membranes.
COMMUNICATION
An Essential Component of a Novel Bacterial Protein Export System
with Homologues in Plastids and Mitochondria
,, and Department of Biological Sciences,
University of Warwick, Coventry CV4 7AL, United Kingdom, the
§ School of Biological Sciences, University of East Anglia,
Norwich NR4 7TJ, United Kingdom, and the ¶ Nitrogen Fixation
Laboratory, John Innes Centre, Colney Lane,
Norwich NR4 7UH, United Kingdom
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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