大肠杆菌的dnaB-dnaC复制蛋白复合体。I. 形成与特性
The dnaB-dnaC replication protein complex of Escherichia coli. I. Formation and properties.
作者信息
Wahle E, Lasken R S, Kornberg A
机构信息
Department of Biochemistry, Stanford University School of Medicine, California 94305-5307.
出版信息
J Biol Chem. 1989 Feb 15;264(5):2463-8.
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.
大肠杆菌的dnaB和dnaC复制蛋白之间形成的复合物通过ATP与dnaC的结合而稳定。dnaB6-dnaC6-ATP6复合物可以在不进行ATP水解的情况下，以低至5×10⁻¹⁰ M的浓度维持。该复合物也可与腺苷5'-(γ-硫代)三磷酸形成，但几乎不产生或不产生dnaB活性，这表明在复合物与DNA结合的后续阶段需要ATP水解。在这一步中，dnaC被释放，留下dnaB在相关DNA上发挥作用。
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