Journal
EUROPEAN JOURNAL OF BIOCHEMISTRY
Volume 268, Issue 12, Pages 3361-3367Publisher
BLACKWELL SCIENCE LTD
DOI: 10.1046/j.1432-1327.2001.02263.x
Keywords
Escherichia coli; Tat protein export pathway; twin-arginine motif; membrane proteins; electron microscopy
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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.
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