Discovery - University of Dundee - Online Publications

Library & Learning Centre

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

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

Research output: Contribution to journalArticle

View graph of relations

Authors

Research units

Info

Original languageEnglish
Pages16717-16722
Number of pages6
JournalJournal of Biological Chemistry
Journal publication date2000
Volume275
Issue22
DOIs
StatePublished

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.

Documents

Library & Learning Centre

Contact | Accessibility | Policy