The archaeal twin-arginine translocation pathway
UNSPECIFIED. (2003) The archaeal twin-arginine translocation pathway. BIOCHEMICAL SOCIETY TRANSACTIONS, 31 (Part 3). pp. 686-689. ISSN 0300-5127Full text not available from this repository.
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 Holobacterium 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.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry|
|Journal or Publication Title:||BIOCHEMICAL SOCIETY TRANSACTIONS|
|Official Date:||June 2003|
|Number of Pages:||4|
|Page Range:||pp. 686-689|
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