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Papers In Press, published online ahead of print March 15, 2000
J. Biol. Chem, 10.1074/jbc.M000800200
Submitted on February 2, 2000
Revised on March 10, 2000
Accepted on March 10, 2000

TatD is a cytoplasmic protein with DNAse activity.No requirement for TatD-family proteins in Sec-independent protein export

Margaret Wexler, Frank Sargent, Rachael L Jack, Nicola R Stanley, Erik G Bogsch, Colin Robinson, Ben C Berks, and Tracy Palmer

Biological Sciences, University of East Anglia, Norwich, Norfolk NR4 7TJ

Corresponding Author: b.berks{at}uea.ac.uk

The Escherichia coli Tat system mediates Sec-independent export of protein precursors bearing twin-arginine signal peptides. Genes known to be involved in this process include tatA, tatB and tatC which form an operon with a fourth gene, tatD. The tatD gene product has two homologues in E. coli coded by the unlinked ycfH and yjjV genes. An E. coli strain with in-frame chromosomal deletions in all three of tatD, ycfH and yjjV exhibits no significant defect in the cellular location of five cofactor-containing enzymes that are synthesised with twin arginine signal peptides. Neither these mutations, nor overproduction of the TatD protein, cause any discernable effect on the export kinetics of an additional E. coli Tat pathway substrate. It is concluded that proteins of the TatD family have no obligate involvement in protein export by the Tat system. TatD is shown to be a cytoplasmic protein that binds divalent metal cations and that exhibits magnesium-dependent nuclease activity. Features of the tatA operon that may control TatD expression are discussed.


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