Twin-arginine-dependent translocation of folded proteins.

Abstract

Twin-arginine translocation (Tat) denotes a protein transport pathway in bacteria, archaea and plant chloroplasts, which is specific for precursor proteins harbouring a characteristic twin-arginine pair in their signal sequences. Many Tat substrates receive cofactors and fold prior to translocation. For a subset of them, proofreading chaperones coordinate maturation and membrane-targeting. Tat translocases comprise two kinds of membrane proteins, a hexahelical TatC-type protein and one or two members of the single-spanning TatA protein family, called TatA and TatB. TatC- and TatA-type proteins form homo- and hetero-oligomeric complexes. The subunits of TatABC translocases are predominantly recovered from two separate complexes, a TatBC complex that might contain some TatA, and a homomeric TatA complex. TatB and TatC coordinately recognize twin-arginine signal peptides and accommodate them in membrane-embedded binding pockets. Advanced binding of the signal sequence to the Tat translocase requires the proton-motive force (PMF) across the membranes and might involve a first recruitment of TatA. When targeted in this manner, folded twin-arginine precursors induce homo-oligomerization of TatB and TatA. Ultimately, this leads to the formation of a transmembrane protein conduit that possibly consists of a pore-like TatA structure. The translocation step again is dependent on the PMF.

DOI: 10.1098/rstb.2011.0202

5 Figures and Tables

0204060201220132014201520162017
Citations per Year

138 Citations

Semantic Scholar estimates that this publication has 138 citations based on the available data.

See our FAQ for additional information.

Cite this paper

@article{Frbel2012TwinargininedependentTO, title={Twin-arginine-dependent translocation of folded proteins.}, author={Julia Fr{\"{o}bel and P. Rose and Matthias P M{\"{u}ller}, journal={Philosophical transactions of the Royal Society of London. Series B, Biological sciences}, year={2012}, volume={367 1592}, pages={1029-46} }