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Tat-dependent protein targeting in prokaryotes and chloroplasts
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UNSPECIFIED (2004) Tat-dependent protein targeting in prokaryotes and chloroplasts. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, 1694 (1-3). pp. 135-147. ISSN 0167-4889
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Official URL: http://dx.doi.org/10.1016/j.bbamcr.2004.03.010
Abstract
The twin-arginine translocation (Tat) system operates in the chloroplast thylakoid mid the plasma membranes of a wide range of bacteria. recognizes substrates bearing cleavable signal peptides in which a twin-arginine motif almost invariably plays a key role in recognition by the translocation machinery. These signal peptides are surprisingly similar to those used to specify, transport by Sec-type systems, but the Tat pathway differs in fundamental respects from Sec-type and other protein translocases. Its key attribute is its ability to translocate large, fully folded (even oligomeric) proteins across tightly sealed membranes. To date. three key fat genes have been characterised and the first details of the Tat system are beginning to emerge. In this article we review the salient features of Tat systems, with an emphasis on the targeting signals involved, the substrate specificities of Tat systems, our current knowledge of Tat complex structures and the known mechanistic features. Although the article is focused primarily on bacterial systems, we incorporate relevant aspects of plant thylakoid Tat work and we discuss how the plant and bacterial systems may differ in some respects. (C) 2004 Elsevier B.V. All rights reserved.
| Item Type: | Journal Item |
|---|---|
| Subjects: | Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology |
| Journal or Publication Title: | BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH |
| Publisher: | ELSEVIER SCIENCE BV |
| ISSN: | 0167-4889 |
| Date: | 11 November 2004 |
| Volume: | 1694 |
| Number: | 1-3 |
| Number of Pages: | 13 |
| Page Range: | pp. 135-147 |
| Identification Number: | 10.1016/j.bbamcr.2004.03.010 |
| Publication Status: | Published |
| URI: | http://wrap.warwick.ac.uk/id/eprint/7500 |
Data sourced from Thomson Reuters' Web of Knowledge
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