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Journal of Bacteriology, December 1998, p. 6519-6528, Vol. 180, No. 24
Department of Bacteriology, University of
Wisconsin
Received 4 June 1998/Accepted 9 October 1998
The oxidative pentose phosphate pathway is required for function of
the alternative pyrimidine biosynthetic pathway, a pathway that allows
thiamine synthesis in the absence of the PurF enzyme in
Salmonella typhimurium. Mutants that no longer required
function of the oxidative pentose phosphate pathway for thiamine
synthesis were isolated. Further phenotypic analyses of these mutants
demonstrated that they were also sensitive to the presence of serine in
the medium, suggesting a partial defect in isoleucine biosynthesis. Genetic characterization showed that these pleiotropic phenotypes were
caused by null mutations in yjgF, a previously
uncharacterized open reading frame encoding a hypothetical 13.5-kDa
protein. The YjgF protein belongs to a class of proteins of unknown
function that exhibit striking conservation across a wide range of
organisms, from bacteria to humans. This work represents the first
detailed phenotypic characterization of yjgF mutants in any
organism and provides important clues as to the function of this highly
conserved class of proteins. Results also suggest a connection between
function of the isoleucine biosynthetic pathway and the requirement for the pentose phosphate pathway in thiamine synthesis.
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Complex Metabolic Phenotypes Caused by a Mutation
in yjgF, Encoding a Member of the Highly Conserved
YER057c/YjgF Family of Proteins
Madison, Madison, Wisconsin 53706
*
Corresponding author. Mailing address: Department of
Bacteriology, University of Wisconsin
Madison, Madison, WI 53706. Phone: (608) 262-2914. Fax: (608) 262-9865. E-mail:
downs{at}macc.wisc.edu.
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