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The dnaB-dnaC replication protein complex of Escherichia coli. I. Formation and properties
E Wahle1, R S Lasken, A Kornberg
1Department of Biochemistry, Stanford University School of Medicine, California 94305-5307.
The Journal of Biological Chemistry
|February 15, 1989
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.