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http://purl.uniprot.org/citations/1370469http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1370469http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1370469http://www.w3.org/2000/01/rdf-schema#comment"We report the molecular cloning and DNA sequence of the gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase. The biotin carboxylase gene encodes a protein of 449 residues that is strikingly similar to amino-terminal segments of two biotin-dependent carboxylase proteins, yeast pyruvate carboxylase and the alpha-subunit of rat propionyl-CoA carboxylase. The deduced biotin carboxylase sequence contains a consensus ATP binding site and a cysteine-containing sequence preserved in all sequenced bicarbonate-dependent biotin carboxylases that may play a key catalytic role. The gene encoding the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase is located upstream of the biotin carboxylase gene and the two genes are cotranscribed. As previously reported by others, the BCCP sequence encoded a protein of 16,688 molecular mass. However, this value is much smaller than that (22,500 daltons) obtained by analysis of the protein. Amino-terminal amino acid sequencing of the purified BCCP protein confirmed the deduced amino acid sequence indicating that BCCP is a protein of atypical physical properties. Northern and primer extension analyses demonstrate that BCCP and biotin carboxylase are transcribed as a single mRNA species that contains an unusually long untranslated leader preceding the BCCP gene. We have also determined the mutational alteration in a previously isolated acetyl-CoA carboxylase (fabE) mutant and show the lesion maps within the BCCP gene and results in a BCCP species defective in acceptance of biotin. Translational fusions of the carboxyl-terminal 110 or 84 (but not 76) amino acids of BCCP to beta-galactosidase resulted in biotinated beta-galactosidase molecules and production of one such fusion was shown to result in derepression of the biotin biosynthetic operon."xsd:string
http://purl.uniprot.org/citations/1370469http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)48362-7"xsd:string
http://purl.uniprot.org/citations/1370469http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)48362-7"xsd:string
http://purl.uniprot.org/citations/1370469http://purl.uniprot.org/core/author"Cronan J.E. Jr."xsd:string
http://purl.uniprot.org/citations/1370469http://purl.uniprot.org/core/author"Cronan J.E. Jr."xsd:string
http://purl.uniprot.org/citations/1370469http://purl.uniprot.org/core/author"Li S.-J."xsd:string
http://purl.uniprot.org/citations/1370469http://purl.uniprot.org/core/author"Li S.-J."xsd:string
http://purl.uniprot.org/citations/1370469http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1370469http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1370469http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/1370469http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/1370469http://purl.uniprot.org/core/pages"855-863"xsd:string
http://purl.uniprot.org/citations/1370469http://purl.uniprot.org/core/pages"855-863"xsd:string
http://purl.uniprot.org/citations/1370469http://purl.uniprot.org/core/title"The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase."xsd:string
http://purl.uniprot.org/citations/1370469http://purl.uniprot.org/core/title"The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase."xsd:string
http://purl.uniprot.org/citations/1370469http://purl.uniprot.org/core/volume"267"xsd:string
http://purl.uniprot.org/citations/1370469http://purl.uniprot.org/core/volume"267"xsd:string
http://purl.uniprot.org/citations/1370469http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1370469
http://purl.uniprot.org/citations/1370469http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1370469
http://purl.uniprot.org/citations/1370469http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/1370469
http://purl.uniprot.org/citations/1370469http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/1370469
http://purl.uniprot.org/uniprot/P24182http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/1370469
http://purl.uniprot.org/uniprot/P0ABD8http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/1370469