title: The Bacillus stearothermophilus replicative helicase: cloning, overexpression and activity.
abstract: As part of biochemical and structural studies of the primosome of a gram positive bacterial species, we describe the cloning of the Bacillus stearothermophilus replicative helicase, DnaB. The protein is 45% and 82% identical to the Escherichia coli and B. subtilis replicative helicases, respectively. Recombinant DnaB was purified and shown to be an active helicase.
authors: Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
authors: L E
authors: LE
authors: Bird
authors: D B
authors: DB
authors: Wigley
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D001483:Base Sequence; D003001:Cloning, Molecular; D004265:DNA Helicases / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*; D053488:DnaB Helicases; D004926:Escherichia coli / Q000235:genetics; D001411:Geobacillus stearothermophilus / Q000201:enzymology* / Q000235:genetics; D008969:Molecular Sequence Data; D016415:Sequence Alignment
chemical_list: D001426:Bacterial Proteins; D004265:DNA Helicases; D053488:DnaB Helicases