Abstract
The ilvC gene product, acetohydroxy acid isomeroreductase, an enzyme essential for isoleucine and valine formation, is subject to substrate induction in Escherichia coli. We have isolated a mutant of E. coli K-12 with a mutation that renders the ilvC gene product noninducible by its substrates, the acetohydroxy acids. This mutation, ilvY466, has been shown to be in a previously undiscovered locus that lies between ilvC and ilvO. The ilvY product, upsilon, is thought to be a regulatory element involved in the induction of ilvC. We postulate the recognition site, ilvQ, or upsilon and suggest that it lies between ilvC and ilvB. A possible model, involving upsilon, in the positive control of isomeroreductase is presented. Pleiotropic effects of the ilvY466 mutation have been recognized from changes in the end-product inhibition of threonine deaminase and of acetohydroxy acid synthetase. In addition, pleiotropic effects of this lesion on the regulation of threonine deaminase and the physical properties of threonine deaminase and acetohydroxy acid synthetase have been observed.
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Selected References
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