The dnaB-dnaC replication protein complex of Escherichia coli. I. Formation and properties.
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.
Wahle
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E
Department of Biochemistry, Stanford University School of Medicine, California 94305-5307.
Lasken
R S
RS
Kornberg
A
A
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
D001426:Bacterial Proteins; D046911:Macromolecular Substances; C022571:adenosine 5'-O-(3-thiotriphosphate); D000255:Adenosine Triphosphate; D005033:Ethylmaleimide