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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.

PMID:2536712
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.

摘要

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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