Affiliation:
1. Department of Bacteriology, University of Wisconsin—Madison, Madison, Wisconsin 53706
Abstract
ABSTRACT
The YjgF/YER057c/UK114 family is a highly conserved class of proteins that is represented in the three domains of life. Thus far, a biochemical function demonstrated for these proteins in vivo or in vitro has yet to be defined. In several organisms, strains lacking a YjgF homolog have a defect in branched-chain amino acid biosynthesis. This study probes the connection between
yjgF
and isoleucine biosynthesis in
Salmonella enterica.
In strains lacking
yjgF
the specific activity of transaminase B, catalyzing the last step in the synthesis of isoleucine, was reduced. In the absence of
yjgF
, transaminase B activity could be restored by inhibiting threonine deaminase, the first enzymatic step in isoleucine biosynthesis. Strains lacking
yjgF
showed an increased sensitivity to sulfometruron methyl, a potent inhibitor of acetolactate synthase. Based on work described here and structural reports in the literature, we suggest a working model in which YjgF has a role in protecting the cell from toxic effects of imbalanced ketoacid pools.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
54 articles.
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