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J. Biol. Chem., Vol. 275, Issue 26, 20096-20103, June 30, 2000
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From the University of Wisconsin School of Pharmacy,
Madison, Wisconsin 53706
IscS, a cysteine desulfurase implicated in the
repair of Fe-S clusters, was recently shown to act as a
sulfurtransferase in the biosynthesis of 4-thiouridine
(s4U) in tRNA (Kambampati, R., and Lauhon, C. T. (1999) Biochemistry 38, 16561-16568). In frame deletion of
the iscS gene in Escherichia coli results in a
mutant strain that lacks s4U in its tRNA. Assays of
cell-free extracts isolated from the iscS
The iscS Gene in Escherichia coli Is
Required for the Biosynthesis of 4-Thiouridine, Thiamin, and NAD*
and
strain confirm the complete loss of tRNA sulfurtransferase activity. In
addition to lacking s4U, the iscS
strain requires thiamin and nicotinic acid for growth in minimal media.
The thiamin requirement can be relieved by the addition of the thiamin
precursor 5-hydroxyethyl-4-methylthiazole, indicating that
iscS is required specifically for thiazole biosynthesis. The growth rate of the iscS strain is half
that of the parent strain in rich medium. When the
iscS strain is switched from rich to minimal
medium containing thiamin and nicotinate, growth is preceded by a
considerable lag period relative to the parent strain. Addition of
isoleucine results in a significant reduction in the duration of this
lag phase. To examine the thiazole requirement, we have reconstituted
the in vitro biosynthesis of ThiS thiocarboxylate, the
ultimate sulfur donor in thiazole biosynthesis, and we show that IscS
mobilizes sulfur for transfer to the C-terminal carboxylate of ThiS.
ThiI, a known factor involved in both thiazole and s4U
synthesis, stimulates this sulfur transfer step by 7-fold. Extracts from the iscS strain show significantly
reduced activity in the in vitro synthesis of ThiS
thiocarboxylate. Transformation of the iscS
strain with an iscS expression plasmid complemented all of
the observed phenotypic effects of the deletion mutant. Of the
remaining two nifS-like genes in E. coli,
neither can complement loss of iscS when each is
overexpressed in the iscS strain. Thus, IscS
plays a significant and specific role at the top of a potentially broad
sulfur transfer cascade that is required for the biosynthesis of
thiamin, NAD, Fe-S clusters, and thionucleosides.
*
This work was supported by National Institutes of Health
Grant GM57002 and a grant from the University of Wisconsin Graduate School.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: University of
Wisconsin School of Pharmacy, 425 N. Charter St., Madison, WI 53706. Tel.: 608-262-3083; Fax: 608-262-3397; E-mail:
clauhon@facstaff.wisc.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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