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The archaeal twin-arginine translocation pathway
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UNSPECIFIED (2003) The archaeal twin-arginine translocation pathway. BIOCHEMICAL SOCIETY TRANSACTIONS, 31 (Part 3). pp. 686-689. ISSN 0300-5127.
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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 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 | ||||
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Subjects: | Q Science > QD Chemistry | ||||
Journal or Publication Title: | BIOCHEMICAL SOCIETY TRANSACTIONS | ||||
Publisher: | PORTLAND PRESS | ||||
ISSN: | 0300-5127 | ||||
Official Date: | June 2003 | ||||
Dates: |
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Volume: | 31 | ||||
Number: | Part 3 | ||||
Number of Pages: | 4 | ||||
Page Range: | pp. 686-689 | ||||
Publication Status: | Published |
Data sourced from Thomson Reuters' Web of Knowledge
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