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

J. Biol. Chem., Vol. 282, Issue 22, 16177-16186, June 1, 2007

This Article Full Text Full Text (PDF) All Versions of this Article: 282/22/16177    most recent M610834200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted 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 Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Leach, M. R. Articles by Zamble, D. B. Search for Related Content PubMed PubMed Citation Articles by Leach, M. R. Articles by Zamble, D. B. Social Bookmarking                      What's this?

The Role of Complex Formation between the Escherichia coli Hydrogenase Accessory Factors HypB and SlyD^*

From the Department of Chemistry, University of Toronto, Toronto, Ontario M5S 3H6, Canada

The Escherichia coli protein SlyD is a member of the FK-506-binding protein family of peptidylprolyl isomerases. In addition to its peptidylprolyl isomerase domain, SlyD is composed of a molecular chaperone domain and a C-terminal tail rich in potential metal-binding residues. SlyD interacts with the [NiFe]-hydrogenase accessory protein HypB and contributes to nickel insertion during biosynthesis of the hydrogenase metallocenter. This study examines the HypB-SlyD complex and its significance in hydrogenase activation. Protein variants were prepared to delineate the interface between HypB and SlyD. Complex formation requires the HypB linker region located between the high affinity N-terminal Ni(II) site and the GTPase domain of the protein. In the case of SlyD, the deletion of a short loop in the chaperone domain abrogates the interaction with HypB. Mutations in either protein that disrupt complex formation in vitro also result in deficient hydrogenase production in vivo, indicating that the contact between HypB and SlyD is important for hydrogenase maturation. Surprisingly, SlyD stimulates release of nickel from the high affinity Ni(II)-binding site of HypB, an activity that is also disrupted by mutations that affect complex formation. Furthermore, a SlyD truncation lacking the C-terminal metal-binding tail still interacts with HypB but is deficient in stimulating metal release and is not functional in vivo. These results suggest that SlyD could activate metal release from HypB during metallation of the [NiFe] hydrogenase.

Received for publication, November 22, 2006 , and in revised form, March 13, 2007.

^* This work was supported in part by funding from the Canadian Institutes of Health Research and the Petroleum Research Fund (American Chemical Society). 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.

¹ Supported by a postdoctoral fellowship from the Natural Sciences and Engineering Research Council of Canada.

² Supported by a Canada Research Chair. To whom correspondence should be addressed: Dept. of Chemistry, University of Toronto, 80 St. George St., Toronto, Ontario M5S 3H6, Canada. Tel.: 416-978-3568; E-mail: dzamble{at}chem.utoronto.ca.

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

This article has been cited by other articles:

				E. L. Benanti and P. T. Chivers An Intact Urease Assembly Pathway Is Required To Compete with NikR for Nickel Ions in Helicobacter pylori J. Bacteriol., April 1, 2009; 191(7): 2405 - 2408. [Abstract] [Full Text] [PDF]

				K. Stingl, K. Schauer, C. Ecobichon, A. Labigne, P. Lenormand, J.-C. Rousselle, A. Namane, and H. de Reuse In Vivo Interactome of Helicobacter pylori Urease Revealed by Tandem Affinity Purification Mol. Cell. Proteomics, December 1, 2008; 7(12): 2429 - 2441. [Abstract] [Full Text] [PDF]

				R. A. Herr, C.-Y. Hung, and G. T. Cole Evaluation of Two Homologous Proline-Rich Proteins of Coccidioides posadasii as Candidate Vaccines against Coccidioidomycosis Infect. Immun., December 1, 2007; 75(12): 5777 - 5787. [Abstract] [Full Text] [PDF]

				J. W. Zhang, M. R. Leach, and D. B. Zamble The Peptidyl-Prolyl Isomerase Activity of SlyD Is Not Required for Maturation of Escherichia coli Hydrogenase J. Bacteriol., November 1, 2007; 189(21): 7942 - 7944. [Abstract] [Full Text] [PDF]