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A gene required for nutritional repression of the Bacillus subtilis dipeptide permease operon
Author(s) -
Slack Frank J.,
Serror Pascale,
Joyce Elizabeth,
Sonenshein Abraham L.
Publication year - 1995
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1995.tb02378.x
Subject(s) - bacillus subtilis , operon , biology , permease , psychological repression , dipeptide , l arabinose operon , gene , biochemistry , microbiology and biotechnology , genetics , bacteria , transporter , amino acid , escherichia coli , gene expression
Summary An insertion mutation was isolated that resulted in derepressed expression of the Bacillus subtilis dipeptide transport operon ( dpp ) during the exponential growth phase in rich medium. DNA flanking the site of insertion was found to encode an operon (codVWXY) of four potential open reading frames (ORFs). The deduced product of the codV ORF is similar to members of the λ Int family; CodW and CodX are homologous to HsIV and HsIU, two putative heat‐shock proteins from Escherichia coli , and to LapC and LapA, two gene products of unknown function from Pasteurella haemolytica. CodX also shares homology with a family of ATPases, including CIpX, a regulatory subunit of the E. coli ClpP protease. CodY does not have any homologues in the databases. The insertion mutation and all previously isolated spontaneous cod mutations were found to map In codY. In‐frame deletion mutations in each of the other cod genes revealed that only codY is required for repression of dpp in nutrient‐rich medium. The cody mutations partially relieved amino acid repression of the histidine utilization (hut) operon but had no effect on regulation of certain other early stationary phase‐induced genes, such as spoVG and gsiA.