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The bacterial twin-arginine translocation pathway.
Lee, Philip A; Tullman-Ercek, Danielle; Georgiou, George.
Affiliation
  • Lee PA; Institute for Cellular and Molecular Biology, Department of Chemical Engineering, University of Texas, Austin, Texas 78712-0231, USA. philipl@che.utexas.edu
Annu Rev Microbiol ; 60: 373-95, 2006.
Article in En | MEDLINE | ID: mdl-16756481
ABSTRACT
The twin-arginine translocation (Tat) pathway is responsible for the export of folded proteins across the cytoplasmic membrane of bacteria. Substrates for the Tat pathway include redox enzymes requiring cofactor insertion in the cytoplasm, multimeric proteins that have to assemble into a complex prior to export, certain membrane proteins, and proteins whose folding is incompatible with Sec export. These proteins are involved in a diverse range of cellular activities including anaerobic metabolism, cell envelope biogenesis, metal acquisition and detoxification, and virulence. The Escherichia coli translocase consists of the TatA, TatB, and TatC proteins, but little is known about the precise sequence of events that leads to protein translocation, the energetic requirements, or the mechanism that prevents the export of misfolded proteins. Owing to the unique characteristics of the pathway, it holds promise for biotechnological applications.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Membrane Transport Proteins / Escherichia coli Proteins Language: En Journal: Annu Rev Microbiol Year: 2006 Type: Article Affiliation country: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Membrane Transport Proteins / Escherichia coli Proteins Language: En Journal: Annu Rev Microbiol Year: 2006 Type: Article Affiliation country: United States