Export of complex cofactor-containing proteins by the bacterial Tat pathway

Palmer, Tracy, Sargent, Frank and Berks, Ben C. (2005) Export of complex cofactor-containing proteins by the bacterial Tat pathway. Trends in Microbiology, 13 (4). pp. 175-180. ISSN 0966-842X

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Abstract

The twin-arginine (Tat) protein translocase is a highly unusual protein transport machine that is dedicated to the movement of folded proteins across the bacterial cytoplasmic membrane. Proteins are targeted to the Tat pathway by means of N-terminal signal peptides harbouring a distinctive twin-arginine motif. In the model organism Escherichia coli, many of the Tat substrates bind redox cofactors that are inserted into apo-proteins before they engage with the Tat machinery. Here we review recent advances in understanding the events involved in the coordination of cofactor insertion with the export process. Current models for Tat protein transport are also discussed.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Biological Sciences
Depositing User:	LivePure Connector
Date Deposited:	01 Mar 2023 16:31
Last Modified:	01 Mar 2023 16:32
URI:	https://ueaeprints.uea.ac.uk/id/eprint/91315
DOI:	10.1016/j.tim.2005.02.002

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