Purified components of the Escherichia coli Tat protein transport system form a double-layered ring structure.
The Escherichia coli twin arginine translocation (Tat) system mediates Sec-independent export of protein precursors bearing twin arginine signal peptides. The genes tatA, tatB, tatC and tatE code for integral membrane proteins that are components of the Tat pathway. Cells co-overexpressing tatABCDE show an increased rate of export of a signal peptide-defective Tat precursor protein and a complex containing the TatA and TatB proteins can be purified from the membranes of such cells. The purified TatAB complex has an apparent molecular mass of 600 kDa as measured by gel permeation chromatography and, like the membranes of wild-type cells, contains a large molar excess of TatA over TatB. Negative stain electron microscopy of the complex reveals cylindrical structures that may correspond to the Tat protein transport channel.
Sargent
F
F
Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences, University of East Anglia, Norwich, UK.
Gohlke
U
U
De Leeuw
E
E
Stanley
N R
NR
Palmer
T
T
Saibil
H R
HR
Berks
B C
BC
D001483:Base Sequence; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure; D017931:DNA Primers; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; D008854:Microscopy, Electron; D011487:Protein Conformation
D002352:Carrier Proteins; D017931:DNA Primers; D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; C408585:twin-arginine translocase complex, E coli