The bacterial twin-arginine translocation pathway

Philip A. Lee*, Danielle Tullman-Ercek, George Georgiou

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapter

238 Scopus citations

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.

Original languageEnglish (US)
Title of host publicationAnnual Review of Microbiology
EditorsNicholas Ornston, Albert Balows, Susan Gottesman, Caroline Harwood
Pages373-395
Number of pages23
DOIs
StatePublished - 2006

Publication series

NameAnnual Review of Microbiology
Volume60
ISSN (Print)0066-4227

Keywords

  • Biotechnology
  • Pathogenesis
  • Protein transport
  • Tat
  • Translocase

ASJC Scopus subject areas

  • Microbiology

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