Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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.

Original publication

DOI

10.1016/j.tim.2005.02.002

Type

Journal article

Journal

Trends Microbiol

Publication Date

04/2005

Volume

13

Pages

175 - 180

Keywords

Bacteria, Bacterial Proteins, Coenzymes, Escherichia coli Proteins, Membrane Transport Proteins, Models, Biological, Protein Folding, Protein Transport