PMID:15817387

Citation	Palmer, T, Sargent, F and Berks, BC (2005) Export of complex cofactor-containing proteins by the bacterial Tat pathway. Trends Microbiol. 13:175-80
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.
Links	PubMed Online version:10.1016/j.tim.2005.02.002
Keywords	Bacteria/genetics; Bacteria/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Coenzymes/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Membrane Transport Proteins/genetics; Membrane Transport Proteins/metabolism; Models, Biological; Protein Folding; Protein Transport/genetics
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.