Protein targeting by the bacterial twin-arginine translocation (Tat) pathway

TY - JOUR

T1 - Protein targeting by the bacterial twin-arginine translocation (Tat) pathway

AU - Berks, Ben C.

AU - Palmer, Tracy

AU - Sargent, Frank

PY - 2005

Y1 - 2005

N2 - The Tat (twin-arginine translocation) protein export system is found in the cytoplasmic membrane of most prokaryotes; and is dedicated to the transport of folded proteins. The Tat system is now known to be essential for many bacterial processes including energy metabolism, cell wall biosynthesis, the nitrogen-fixing symbiosis and bacterial pathogenesis. Recent studies demonstrate that substrate-specific accessory proteins prevent improperly assembled substrates from interacting with the Tat transporter. During the transport cycle itself substrate proteins bind to a receptor complex in the membrane which then recruits a protein-translocating channel to carry out the transport reaction.

AB - The Tat (twin-arginine translocation) protein export system is found in the cytoplasmic membrane of most prokaryotes; and is dedicated to the transport of folded proteins. The Tat system is now known to be essential for many bacterial processes including energy metabolism, cell wall biosynthesis, the nitrogen-fixing symbiosis and bacterial pathogenesis. Recent studies demonstrate that substrate-specific accessory proteins prevent improperly assembled substrates from interacting with the Tat transporter. During the transport cycle itself substrate proteins bind to a receptor complex in the membrane which then recruits a protein-translocating channel to carry out the transport reaction.

U2 - 10.1016/j.mib.2005.02.010

DO - 10.1016/j.mib.2005.02.010

M3 - Article

C2 - 15802249

SN - 1369-5274

VL - 8

SP - 174

EP - 181

JO - Current Opinion in Microbiology

JF - Current Opinion in Microbiology

IS - 2

ER -