HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 278, Issue 35, 32501-32506, August 29, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/35/32501    most recent M301076200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Papish, A. L. Articles by Turner, R. J. Search for Related Content PubMed PubMed Citation Articles by Papish, A. L. Articles by Turner, R. J. Social Bookmarking                      What's this?

The Twin-arginine Leader-binding Protein, DmsD, Interacts with the TatB and TatC Subunits of the Escherichia coli Twin-arginine Translocase^*

Andriyka L. Papish , Carol L. Ladner and Raymond J. Turner 

From the Department of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada

The twin-arginine translocase (Tat) pathway is involved in the targeting and translocation of fully folded proteins to the inner membrane and periplasm of bacteria. Proteins that use this pathway contain a characteristic twin-arginine signal sequence, which interacts with the receptor complex formed by the TatBC subunits. Recently, the DmsD protein was discovered, which binds to the twin-arginine signal sequences of the anaerobic respiratory enzymes dimethylsulfoxide reductase (DmsABC) and trimethylamine N-oxide (TMAO) reductase. In this work, the targeting of DmsD within Escherichia coli was investigated. Using cell fractionation and Western blot analysis, DmsD is found to be associated with the inner membrane of wild-type E. coli and a dmsABC mutant E. coli under anaerobic conditions. In contrast, DmsD is predominantly found in the cytoplasmic fraction of a tatABCDE strain, which suggests that DmsD interacts with the membrane-associated Tat complex. Under aerobic conditions DmsD was also found primarily in the cytoplasmic fraction of wild-type E. coli, suggesting that physiological conditions have a significant effect upon the targeting of DmsD to the inner membrane. Size exclusion chromatography data and membrane washing studies indicate that DmsD is interacting tightly with an integral membrane protein and not with the lipid component of the E. coli inner membrane. Additional investigation into the nature of this interaction revealed that the TatB and TatC subunits of the translocase are important for the interaction of DmsD with the E. coli inner membrane.

Received for publication, January 31, 2003 , and in revised form, June 13, 2003.

^* This research was supported by an operating grant (to R. J. T.) by the Canadian Institute for Health Research. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by studentships from the Natural Sciences and Engineering Research Council of Canada, Alberta Heritage Foundation for Medical Research, and from the Informatics Centre of Research Excellence (iCORE).

To whom correspondence should be addressed: Dept. of Biological Sciences, University of Calgary, 2500 University Drive N.W., Calgary, Alberta T2N 1N4, Canada. Tel.: 403-220-4308; Fax: 403-289-9311; E-mail: turnerr{at}ucalgary.ca.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				F. Sargent Constructing the wonders of the bacterial world: biosynthesis of complex enzymes Microbiology, March 1, 2007; 153(3): 633 - 651. [Abstract] [Full Text] [PDF]

				U. Lindenstrauss and T. Bruser Conservation and Variation between Rhodobacter capsulatus and Escherichia coli Tat Systems J. Bacteriol., November 15, 2006; 188(22): 7807 - 7814. [Abstract] [Full Text] [PDF]

				K. Hatzixanthis, T. A. Clarke, A. Oubrie, D. J. Richardson, R. J. Turner, and F. Sargent Signal peptide-chaperone interactions on the twin-arginine protein transport pathway PNAS, June 14, 2005; 102(24): 8460 - 8465. [Abstract] [Full Text] [PDF]

				M. Ilbert, V. Mejean, and C. Iobbi-Nivol Functional and structural analysis of members of the TorD family, a large chaperone family dedicated to molybdoproteins Microbiology, April 1, 2004; 150(4): 935 - 943. [Abstract] [Full Text] [PDF]

				M. P. DeLisa, P. Lee, T. Palmer, and G. Georgiou Phage Shock Protein PspA of Escherichia coli Relieves Saturation of Protein Export via the Tat Pathway J. Bacteriol., January 15, 2004; 186(2): 366 - 373. [Abstract] [Full Text] [PDF]