The clamp-loader-helicase interaction in Bacillus.: Atomic force microscopy reveals the structural organisation of the DnaB-Ï„ complex in Bacillus
The clamp-loader-helicase interaction in Bacillus.: Atomic force microscopy reveals the structural organisation of the DnaB-Ï„ complex in Bacillus
复制标题
芽孢杆菌中钳夹-装载器-螺旋酶的相互作用 原子力显微镜揭示芽孢杆菌中DnaB-Ï "复合体的结构组织
DOI：
10.1016/j.jmb.2003.12.043
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发表时间：
2004-02-13
影响因子：
5.6
通讯作者：
Soultanas, P
中科院分区：
文献类型：
--
作者：
Haroniti, A;Anderson, C;Soultanas, P
夹钳-装载机-解旋酶相互作用是复制体的一个重要特征。尽管对大肠杆菌中的夹子-加载器-夹子-DNA聚合酶α相互作用进行了重要的生化和结构研究，但相比之下，对夹子-加载器-解旋酶相互作用知之甚少。夹钳装载机的 tau 亚基介导与 DnaB 的相互作用。我们最近在芽孢杆菌系统中表征了这种相互作用，并建立了 tau(5)-DnaB(6) 化学计量。在这里，我们获得了 tau-DnaB 复合物的原子力显微镜图像，首次揭示了其结构的结构。我们发现，尽管芽孢杆菌中不存在较短的 γ 版本，但 tau 蛋白具有与大肠杆菌类似的结构域组织，并且拥有与 DnaB 相互作用的等效 C 端结构域。 DnaB 的相互作用界面也位于其 C 端结构域。综合数据有助于我们对细菌复制体的理解。 (C) 2003 Elsevier Ltd. 保留所有权利。
The clamp-loader-helicase interaction is an important feature of the replisome. Although significant biochemical and structural work has been carried out on the clamp-loader-clamp-DNA polymerase alpha interactions in Escherichia coli, the clamp-loader-helicase interaction is poorly understood by comparison. The tau subunit of the clamp-loader mediates the interaction with DnaB. We have recently characterised this interaction in the Bacillus system and established a tau(5)-DnaB(6) stoichiometry. Here, we have obtained atomic force microscopy images of the tau-DnaB complex that reveal the first structural insight into its architecture. We show that despite the reported absence of the shorter gamma version in Bacillus, tau has a domain Organisation similar to its E. coli counterpart and possesses an equivalent C-terminal domain that interacts with DnaB. The interaction interface of DnaB is also localised in its C-terminal domain. The combined data contribute towards our understanding of the bacterial replisome. (C) 2003 Elsevier Ltd. All rights reserved.