title: Transcriptional analysis of bglPH expression in Bacillus subtilis: evidence for two distinct pathways mediating carbon catabolite repression.
abstract: In Bacillus subtilis, aryl-beta-glucosides such as salicin and arbutin are catabolized by the gene products of bglP and bglH, encoding an enzyme II of the phosphoenolpyruvate sugar-phosphotransferase system and a phospho-beta-glucosidase, respectively. These two genes are transcribed from a single promoter. The presence of a transcript of about 4,000 nucleotides detected by Northern (RNA) blot analysis indicates that bglP and bglH are part of an operon. However, this transcript is only present when cells are grown in the presence of the inducing substrate, salicin. In the absence of the inducer, a transcript of about 110 nucleotides can be detected, suggesting that transcription terminates downstream of the promoter at a stable termination structure. Initiation of transcription is abolished in the presence of rapidly metabolized carbon sources. Catabolite repression of bglPH expression involves the trans-acting factors CcpA and HPr. In a ccpA mutant, transcription initiation is relieved from glucose repression. Furthermore, we report a catabolite responsive element-CcpA-independent form of catabolite repression requiring the ribonucleic antiterminator-terminator region, which is the target of antitermination, and the wild-type HPr protein of the phosphotransferase system. Evidence that the antitermination protein LicT is a crucial element for this type of regulation is provided.
authors.affiliation: Institut für Mikrobiologie und Molekularbiologie, Ernst-Moritz-Arndt Universität Greifswald, Germany.
authors.forename: S
authors.initials: S
authors.lastname: Krüger
authors.forename: S
authors.initials: S
authors.lastname: Gertz
authors.forename: M
authors.initials: M
authors.lastname: Hecker
mesh_terms: D001412:Bacillus subtilis / Q000235:genetics*; D001426:Bacterial Proteins / Q000502:physiology; D001483:Base Sequence; D001592:Benzyl Alcohols / Q000494:pharmacology; D004268:DNA-Binding Proteins / Q000502:physiology; D004790:Enzyme Induction; D004794:Enzyme Repression; D015964:Gene Expression Regulation, Bacterial / Q000187:drug effects / Q000502:physiology*; D005947:Glucose / Q000494:pharmacology; D005959:Glucosidases / Q000096:biosynthesis / Q000235:genetics*; D005960:Glucosides; D008957:Models, Genetic; D008969:Molecular Sequence Data; D009154:Mutation; D009876:Operon / Q000235:genetics; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000096:biosynthesis / Q000235:genetics* / Q000502:physiology; D012329:RNA, Bacterial; D012333:RNA, Messenger / Q000096:biosynthesis; D012097:Repressor Proteins / Q000502:physiology; D014157:Transcription Factors / Q000502:physiology; D014158:Transcription, Genetic / Q000187:drug effects / Q000502:physiology*
chemical_list: D001426:Bacterial Proteins; D001592:Benzyl Alcohols; D004268:DNA-Binding Proteins; D005960:Glucosides; C098955:LicT protein, Bacteria; D012329:RNA, Bacterial; D012333:RNA, Messenger; D012097:Repressor Proteins; D014157:Transcription Factors; C069286:catabolite control proteins, bacteria; C005696:salicin; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C030182:phosphocarrier protein HPr; C031629:phosphoenolpyruvate-glucose phosphotransferase; D005959:Glucosidases; C066586:6-phospho-beta-glucosidase; D005947:Glucose