The archaeal twin-arginine translocation pathway.
Biochem Soc Trans, 2003/6;31(Pt 3):686-9.
Hutcheon GW[1], Bolhuis A
Affiliations
PMID: 12773183
Impact factor: 4.919
Abstract
The twin-arginine translocation (Tat) pathway is a system with the unique ability to export proteins in a fully folded conformation. Its main components are TatA, TatB and TatC, all of which are required for Tat-dependent export. The Tat pathway is found in several Archaea, and in most of them a moderate number of predicted Tat-dependent substrates are present. Putative substrates include those binding cofactors such as iron-sulphur clusters and molybdopterin. In these Archaea, the role of the Tat pathway seems to be similar to that of bacteria: the export of a small subset of proteins that fold before translocation across the cytoplasmic membrane. The exception to this is the Tat system of the halophilic archaeon Halobacterium sp. NRC-1. In this organism, the majority of extra-cytoplasmic proteins are predicted to use the Tat pathway, which is, most likely, a specific adaptation to its particular lifestyle in highly saline conditions.
MeSH terms
Amino Acid Sequence; Archaea; Archaeal Proteins; Arginine; Bacteria; Biological Transport; Chloroplasts; Molecular Sequence Data; Sequence Alignment; Sequence Homology, Amino Acid
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