The bacterial twin-arginine translocation pathway
Philip A Lee1, Danielle Tullman-Ercek, George Georgiou
1Institute for Cellular and Molecular Biology, Department of Chemical Engineering, University of Texas, Austin, Texas 78712-0231, USA. philipl@che.utexas.edu
Annual Review of Microbiology
|June 8, 2006
Summary
The twin-arginine translocation (Tat) pathway exports folded proteins across bacterial membranes. Understanding this pathway is crucial for its biotechnological applications.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- The twin-arginine translocation (Tat) pathway facilitates the export of folded proteins across the bacterial cytoplasmic membrane.
- Tat pathway substrates encompass redox enzymes, multimeric proteins, membrane proteins, and proteins with Sec export-incompatible folding.
Purpose of the Study:
- To elucidate the mechanisms and energetic requirements of the Tat pathway in protein translocation.
- To investigate how the Tat pathway prevents the export of misfolded proteins.
Main Methods:
- The study focuses on the Escherichia coli Tat translocase, composed of TatA, TatB, and TatC proteins.
- Investigates the sequence of events, energetic demands, and specificity of the Tat pathway.
Main Results:
- Identifies key protein substrates and their diverse cellular roles, including anaerobic metabolism, cell envelope biogenesis, metal homeostasis, and virulence.
- Highlights the limited knowledge regarding the precise translocation steps and anti-misfolding mechanisms.
Conclusions:
- The Tat pathway is essential for exporting specific folded proteins critical for various bacterial functions.
- The unique nature of the Tat pathway presents significant potential for biotechnological advancements.
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