Abstract
Bacillus subtilis mutants deficient in amino acid repression of the histidine utilization (hut) operon were isolated by transposon mutagenesis. Genetic characterization of these mutants indicated that they most likely contained transposon insertions within the codVWXY operon. The codY gene is required for nutritional regulation of the dipeptide permease (dpp) operon. An examination of hut expression in a delta codY mutant demonstrated that amino acid repression exerted at the hutOA operator, which lies immediately downstream of the hut promoter, was defective in a delta codY mutant. The codY gene product was not required for amino acid regulation of either hut induction or the expression of proline oxidase, the first enzyme in proline degradation. This indicates that more than one mechanism of amino acid repression is present in B. subtilis. An examination of dpp and hut expression in cells during exponential growth in various media revealed that the level of CodY-dependent regulation appeared to be related to the growth rate of the culture.
MeSH Terms
Amino Acids/metabolism
Bacillus subtilis/genetics
Bacterial Proteins/physiology
Carbon/metabolism
DNA-Binding Proteins
Gene Expression Regulation, Bacterial
Histidine/metabolism
Membrane Transport Proteins/genetics
Mutation
Operon
Proline/metabolism
Repressor Proteins/physiology
Trans-Activators
Chemicals
Amino Acids
Bacterial Proteins
DNA-Binding Proteins
Membrane Transport Proteins
Repressor Proteins
Trans-Activators
oligopeptide permease, Bacteria
Histidine
Carbon
Proline
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Fisher S H
Department of Microbiology, Boston University School of Medicine, Massachusetts 02118, USA.
Rohrer K
Ferson A E
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