Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 35, Issue -, Pages 835-847Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST0350835
Keywords
membrane protein; membrane transport; molecular chaperone; protein-protein interaction; protein targeting; twin-arginine translocase
Categories
Funding
- Biotechnology and Biological Sciences Research Council [BBS/B/07780/2] Funding Source: researchfish
- Biotechnology and Biological Sciences Research Council [BBS/B/07780/2] Funding Source: Medline
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The Tat (twin-arginine transport) pathway is a protein-targeting system dedicated to the transmembrane translocation of fully folded proteins. This system is highly prevalent in the cytoplasmic membranes of bacteria and archaea, and is also found in the thylakoid membranes of plant chloroplasts and possibly also in the inner membrane of plant mitochondria. Proteins are targeted to a membrane-embedded Tat translocase by specialized N-terminal twin-arginine signal peptides bearing an SRRXFLK amino acid motif. The genes encoding components of the Tat translocase were discovered approx. 10 years ago, and, since then, research in this area has expanded on a global scale. in this review, the key discoveries in this field are summarized, and recent studies of bacterial twin-arginine signal-peptide-binding proteins are discussed.
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