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Originally published In Press as doi:10.1074/jbc.M301577200 on March 31, 2003
J. Biol. Chem., Vol. 278, Issue 23, 20708-20715, June 6, 2003
The YggX Protein of Salmonella enterica Is Involved in Fe(II) Trafficking and Minimizes the DNA Damage Caused by Hydroxyl Radicals
RESIDUE CYS-7 IS ESSENTIAL FOR YggX FUNCTION*
Jeffrey A. Gralnick and
Diana M. Downs
From the
Department of Bacteriology, University of Wisconsin-Madison, Madison,
Wisconsin 53706
Previous work from our laboratory identified YggX as a protein whose
accumulation increased the resistance of Salmonella enterica to
superoxide stress, reversed defects attributed to oxidized [Fe-S] clusters,
and decreased the spontaneous mutation frequency of the cells. Here we present
work aimed at determining why the accumulation of YggX correlates with reduced
mutation frequency. Genetic and biochemical data showed that accumulation of
YggX reduced the damage to DNA by hydroxyl radicals. The ability of purified
YggX to protect DNA from Fenton chemistry mediated damage in vitro
and to decrease the concentration of Fe(II) ions in solution available for
chelation provided a framework for the interpretation of data obtained from
in vivo experiments. The interpretation of in vitro assay
results, within the context of the in vivo phenotypes, was validated
by a mutant variant of YggX (C7S) that was unable to function in vivo
or in vitro. We propose a model, based on data presented here and
reported earlier, that suggests YggX is a player in Fe(II) trafficking in
bacteria.
Received for publication, February 13, 2003
, and in revised form, March 28, 2003.
* This work was supported in part by National Science Foundation Grant
MCB0096513 and National Institutes of Health Grant GM47296. The J. S.
McDonnell Foundation also provided funds from a 21st Century Scientist
Scholars Award. 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 the Jerome J. Stefaniak Predoctoral Fellowship from the
Department of Bacteriology.
To whom correspondence should be addressed: Dept. of Bacteriology, 1550 Linden
Dr., Madison, WI 53706. Tel.: 608-265-4630; Fax: 608-262-9865; E-mail:
downs{at}bact.wisc.edu.

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Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.
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