title: Regulation of the putative bglPH operon for aryl-beta-glucoside utilization in Bacillus subtilis.
abstract: The expression of the putative operon bglPH of Bacillus subtilis was studied by using bglP'-lacZ transcriptional fusions. The bglP gene encodes an aryl-beta-glucoside-specific enzyme II of the phosphoenolpyruvate sugar:phosphotransferase system, whereas the bglH gene product functions as a phospho-beta-glucosidase. Expression of bglPH is regulated by at least two different mechanisms: (i) carbon catabolite repression and (ii) induction via an antitermination mechanism. Distinct deletions of the promoter region were created to determine cis-acting sites for regulation. An operatorlike structure partially overlapping the -35 box of the promoter of bglP appears to be the catabolite-responsive element of this operon. The motif is similar to that of amyO and shows no mismatches with respect to the consensus sequence established as the target of carbon catabolite repression in B. subtilis. Catabolite repression is abolished in both ccpA and ptsH1 mutants. The target of the induction by the substrate, salicin or arbutin, is a transcriptional terminator located downstream from the promoter of bglP. This structure is very similar to that of transcriptional terminators which regulate the induction of the B. subtilis sacB gene, the sacPA operon, and the Escherichia coli bgl operon. The licT gene product, a member of the BglG-SacY family of antitermination proteins, is essential for the induction process. Expression of bglP is under the negative control of its own gene product. The general proteins of the phosphoenolpyruvate-dependent phosphotransferase system are required for bglP expression. Furthermore, the region upstream from bglP, which reveals a high AT content, exerts a negative regulatory effect on bglP expression.
authors.affiliation: Institut für Mikrobiologie und Molekularbiologie, Ernst-Moritz-Arndt-Universität, Greifswald, Germany.
authors.forename: S
authors.initials: S
authors.lastname: Krüger
authors.forename: M
authors.initials: M
authors.lastname: Hecker
mesh_terms: D001104:Arbutin / Q000494:pharmacology; D001412:Bacillus subtilis / Q000235:genetics* / Q000378:metabolism; D001426:Bacterial Proteins; D001483:Base Sequence; D001592:Benzyl Alcohols / Q000494:pharmacology; D004268:DNA-Binding Proteins / Q000235:genetics; D004790:Enzyme Induction / Q000187:drug effects; D004794:Enzyme Repression; D015964:Gene Expression Regulation, Bacterial / Q000235:genetics*; D005959:Glucosidases / Q000235:genetics*; D005960:Glucosides / Q000378:metabolism*; D008969:Molecular Sequence Data; D009875:Operator Regions, Genetic / Q000235:genetics; D009876:Operon / Q000235:genetics; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000096:biosynthesis / Q000235:genetics*; D011401:Promoter Regions, Genetic / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis; D012097:Repressor Proteins / Q000235:genetics; D017384:Sequence Deletion; D013728:Terminator Regions, Genetic
chemical_list: D001426:Bacterial Proteins; D001592:Benzyl Alcohols; D004268:DNA-Binding Proteins; D005960:Glucosides; D011993:Recombinant Fusion Proteins; D012097:Repressor Proteins; C069286:catabolite control proteins, bacteria; C005696:salicin; D001104:Arbutin; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C031629:phosphoenolpyruvate-glucose phosphotransferase; D005959:Glucosidases; C066586:6-phospho-beta-glucosidase