The twin-arginine translocation (Tat) protein export pathway

TY - JOUR

T1 - The twin-arginine translocation (Tat) protein export pathway

A1 - Palmer,Tracy

A1 - Berks,Ben C.

AU - Palmer,Tracy

AU - Berks,Ben C.

PY - 2012

Y1 - 2012

N2 - The twin-arginine translocation (Tat) protein export system is present in the cytoplasmic membranes of most bacteria and archaea and has the highly unusual property of transporting fully folded proteins. The system must therefore provide a transmembrane pathway that is large enough to allow the passage of structured macromolecular substrates of different sizes but that maintains the impermeability of the membrane to ions. In the Gram-negative bacterium Escherichia coli, this complex task can be achieved by using only three small membrane proteins: TatA, TatB and TatC. In this Review, we summarize recent advances in our understanding of how this remarkable machine operates. © 2012 Macmillan Publishers Limited. All rights reserved.

AB - The twin-arginine translocation (Tat) protein export system is present in the cytoplasmic membranes of most bacteria and archaea and has the highly unusual property of transporting fully folded proteins. The system must therefore provide a transmembrane pathway that is large enough to allow the passage of structured macromolecular substrates of different sizes but that maintains the impermeability of the membrane to ions. In the Gram-negative bacterium Escherichia coli, this complex task can be achieved by using only three small membrane proteins: TatA, TatB and TatC. In this Review, we summarize recent advances in our understanding of how this remarkable machine operates. © 2012 Macmillan Publishers Limited. All rights reserved.

UR - http://www.scopus.com/inward/record.url?partnerID=yv4JPVwI&eid=2-s2.0-84862501228&md5=ff5f4a79281c238932b2f431e6226d48

U2 - 10.1038/nrmicro2814

DO - 10.1038/nrmicro2814

M1 - Article

JO - Nature Reviews Microbiology

JF - Nature Reviews Microbiology

SN - 1740-1526

IS - 7

VL - 10

SP - 483

EP - 496

ER -