Journal
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 84
Volume 84, Issue -, Pages 843-864Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-biochem-060614-034251
Keywords
protein transport; twin-arginine; membrane protein; signal peptide; bacterial protein export; thylakoid import
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Funding
- Biotechnology and Biological Sciences Research Council Funding Source: Medline
- Medical Research Council [MR/L000776/1, MR/K000721/1] Funding Source: Medline
- BBSRC [BB/L002531/1] Funding Source: UKRI
- MRC [MR/L000776/1, MR/K000721/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/L002531/1] Funding Source: researchfish
- Medical Research Council [MR/L000776/1, MR/K000721/1] Funding Source: researchfish
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The twin-arginine translocation (Tat) system, found in prokaryotes, chloroplasts, and sonic mitochondria, allows folded proteins to be moved across membranes. How this transport is achieved without significant ion leakage is an intriguing mechanistic question. Tat transport is mediated by complexes formed from small integral membrane proteins from just two protein families. Atomic-resolution structures have recently been determined for representatives of both these protein families, providing the first molecular-level glimpse of the Tat machinery. I review our current understanding of the mechanism of Tat transport in light of these new structural data.
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