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, Tracy Palmer

    Research output: Contribution to journalArticle

    208 Citations (Scopus)

    Abstract

    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 that 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 synthesized with twin arginine signal peptides. Neither these mutations nor overproduction of the TatD protein cause any discernible 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. TatD binds to immobilized Ni(2+) or Zn(2+) affinity columns and exhibits magnesium-dependent DNase activity. Features of the tatA operon that may control TatD expression are discussed.
    Original languageEnglish
    Pages (from-to)16717-16722
    Number of pages6
    JournalJournal of Biological Chemistry
    Volume275
    Issue number22
    DOIs
    Publication statusPublished - 2000

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