title: Analysis of CcpA mutations defective in carbon catabolite repression in Bacillus megaterium.
abstract: Five mutations in ccpA of Bacillus megaterium with impaired functions were analysed for carbon catabolite repression. The phenotypes support the hypothesis that CcpA assumes a PurR/LacI fold. The completely inactive mutants CcpA119GE and CcpA326am cause alterations which are incompatible with that fold. A mutation with reduced activity, CcpA81GE, affects a site that would be partially surface exposed and may interfere with structure formation or cofactor binding. A mutation in the putative hinge alpha-helix, CcpA52AE, is negative transdominant over wild-type ccpA. The mutant CcpA38am is inactive, although reduced amounts of wild-type size protein are produced.
authors.affiliation: Lehrstuhl für Mikrobiologie, Friedrick-Alexander Universität Erlangen-Nümberg, FRG.
authors.forename: A
authors.initials: A
authors.lastname: Kraus
authors.forename: W
authors.initials: W
authors.lastname: Hillen
mesh_terms: D001410:Bacillus megaterium / Q000235:genetics* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry; D002244:Carbon / Q000378:metabolism*; D004252:DNA Mutational Analysis; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000235:genetics*; D004794:Enzyme Repression / Q000235:genetics*; D015964:Gene Expression Regulation, Bacterial / Q000235:genetics; D005798:Genes, Bacterial; D005799:Genes, Dominant; D005947:Glucose / Q000378:metabolism; D009154:Mutation / Q000235:genetics*; D012097:Repressor Proteins / Q000737:chemistry / Q000235:genetics*; D014994:Xylose / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; C065825:PurR protein, Bacteria; D012097:Repressor Proteins; C069286:catabolite control proteins, bacteria; D002244:Carbon; D014994:Xylose; D005947:Glucose