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

J. Biol. Chem., Vol. 282, Issue 14, 10352-10359, April 6, 2007

This Article Full Text Full Text (PDF) All Versions of this Article: 282/14/10352    most recent M610656200v1 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 Justino, M. C. Articles by Saraiva, L. M. Search for Related Content PubMed PubMed Citation Articles by Justino, M. C. Articles by Saraiva, L. M. Social Bookmarking                      What's this?

Escherichia coli Di-iron YtfE Protein Is Necessary for the Repair of Stress-damaged Iron-Sulfur Clusters^*

From the Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Avenida da República, 2780-157 Oeiras, Portugal

DNA microarray experiments showed that the expression of the Escherichia coli ytfE gene is highly increased upon exposure to nitric oxide. We also reported that deletion of ytfE significantly alters the phenotype of E. coli, generating a strain with enhanced susceptibility to nitrosative stress and defective in the activity of several iron-sulfur-containing proteins. In this work, it is shown that the E. coli ytfE confers protection against oxidative stress. Furthermore, we found that the damage of the [4Fe-4S]²⁺ clusters of aconitase B and fumarase A caused by exposure to hydrogen peroxide and nitric oxide stress occurs at higher rates in the absence of ytfE. The ytfE null mutation also abolished the recovery of aconitase and fumarase activities, which is observed in wild type E. coli once the stress is scavenged. Notably, upon the addition of purified holo-YtfE protein to the mutant cell extracts, the enzymatic activities of fumarase and aconitase are fully recovered and at rates similar to the wild type strain. We concluded that YtfE is critical for the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions.

Received for publication, November 16, 2006 , and in revised form, February 7, 2007.

^* This work was supported by Fundação para a Ciência e Tecnologia (FCT) Projects POCTI/2002/BME/44597 and POCI/SAU-IMI/56088/2004. 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 Recipient of FCT Grant SFRH/BD/13756/2003.

² To whom correspondence should be addressed. Tel.: 351-214469328; Fax: 351-214411277; E-mail: lst{at}itqb.unl.pt.

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

This article has been cited by other articles:

				T. W. Overton, M. C. Justino, Y. Li, J. M. Baptista, A. M. P. Melo, J. A. Cole, and L. M. Saraiva Widespread Distribution in Pathogenic Bacteria of Di-Iron Proteins That Repair Oxidative and Nitrosative Damage to Iron-Sulfur Centers J. Bacteriol., March 15, 2008; 190(6): 2004 - 2013. [Abstract] [Full Text] [PDF]

				C. Ayala-Castro, A. Saini, and F. W. Outten Fe-S Cluster Assembly Pathways in Bacteria Microbiol. Mol. Biol. Rev., March 1, 2008; 72(1): 110 - 125. [Abstract] [Full Text] [PDF]

				V. Isabella, L. F. Wright, K. Barth, J. M. Spence, S. Grogan, C. A. Genco, and V. L. Clark cis- and trans-acting elements involved in regulation of norB (norZ), the gene encoding nitric oxide reductase in Neisseria gonorrhoeae Microbiology, January 1, 2008; 154(1): 226 - 239. [Abstract] [Full Text] [PDF]

				K. Strube, S. de Vries, and R. Cramm Formation of a Dinitrosyl Iron Complex by NorA, a Nitric Oxide-binding Di-iron Protein from Ralstonia eutropha H16 J. Biol. Chem., July 13, 2007; 282(28): 20292 - 20300. [Abstract] [Full Text] [PDF]