The dnaB-dnaC replication protein complex of Escherichia coli. II. Role of the complex in mobilizing dnaB functions.
The dnaB-dnaC replication protein complex of Escherichia coli. II. Role of the complex in mobilizing dnaB functions.
复制标题
大肠杆菌的 dnaB-dnaC 复制蛋白复合物。
DOI：
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发表时间：
1989
影响因子：
4.8
通讯作者：
A. Kornberg
中科院分区：
文献类型：
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作者：
E. Wahle;R. Lasken;A. Kornberg
大肠杆菌的 dnaC 蛋白通过与 dnaB 蛋白形成复合物，促进与单链 DNA 的相互作用，使 dnaB 能够发挥其 ATP 酶、解旋酶和引发功能。在 dnaB-dnaC 复合物中，dnaB 似乎不活跃，但在 ATP 依赖性从复合物中释放 dnaC 后变得活跃。当腺苷 5'-(γ-硫代)三磷酸取代 ATP 时，dnaB-dnaC 复合物不会引导 dnaB 发挥其目标作用。过量的 dnaC 会抑制 dna beta 的作用并增强 ATP gamma S 的作用。在 dnaA 蛋白驱动的双链染色体复制起始过程中，dnaB 通过 dnaB-dnaC 复合体引入，发挥其重要的解旋酶作用。类似地，当 dnaA 蛋白与单链 DNA 非特异性相互作用时，dnaB-dnaC 复合物对于引入 dnaB 至关重要，因为它在引物酶形成引物中发挥作用。
The dnaC protein of Escherichia coli, by forming a complex with the dnaB protein, facilitates the interactions with single-stranded DNA that enable dnaB to perform its ATPase, helicase, and priming functions. Within the dnaB-dnaC complex, dnaB appears to be inactive but becomes active upon the ATP-dependent release of dnaC from the complex. With adenosine 5'-(gamma-thio)triphosphate substituted for ATP, the dnaB-dnaC complex does not direct dnaB to its targeted actions. Excess dnaC inhibits dna beta actions and augments the ATP gamma S effects. In the dnaA protein-driven initiation of duplex chromosome replication, dnaB is introduced for its essential helicase role via the dnaB-dnaC complex. Similarly, when the dnaA protein interacts nonspecifically with single-stranded DNA, the dnaB-dnaC complex is essential to introduce dnaB for its role in primer formation by primase.