title: The dnaB-dnaC replication protein complex of Escherichia coli. I. Formation and properties.
abstract: The complex formed between the dnaB and dnaC replication proteins of Escherichia coli is stabilized by ATP binding to dnaC. The dnaB6-dnaC6-ATP6 complex can be maintained without ATP hydrolysis at a concentration as low as 5 x 10(-10) M. The complex is also formed with adenosine 5'-(gamma-thio)triphosphate but generates little or no dnaB activity, suggesting a requirement for ATP hydrolysis in the subsequent stage of binding of the complex to DNA. In this step, dnaC is released, leaving dnaB to function on the associated DNA.
authors.affiliation: Department of Biochemistry, Stanford University School of Medicine, California 94305-5307.
authors.forename: E
authors.initials: E
authors.lastname: Wahle
authors.forename: R S
authors.initials: RS
authors.lastname: Lasken
authors.forename: A
authors.initials: A
authors.lastname: Kornberg
mesh_terms: D000255:Adenosine Triphosphate / Q000031:analogs & derivatives / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D004261:DNA Replication; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D005033:Ethylmaleimide / Q000494:pharmacology; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight
chemical_list: D001426:Bacterial Proteins; D046911:Macromolecular Substances; C022571:adenosine 5'-O-(3-thiotriphosphate); D000255:Adenosine Triphosphate; D005033:Ethylmaleimide