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首页> 外文期刊>EMBO Journal >Bacterial actin: architecture of the ParMRC plasmid DNA partitioning complex
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Bacterial actin: architecture of the ParMRC plasmid DNA partitioning complex

机译:细菌肌动蛋白:ParMRC的架构质粒DNA分区复杂

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摘要

The R1 plasmid employs ATP-driven polymerisation of the actin-like protein ParM to move newly replicated DNA to opposite poles of a bacterial cell. This process is essential for ensuring accurate segregation of the low-copy number plasmid and is the best characterised example of DNA partitioning in prokaryotes. In vivo, ParM only forms long filaments when capped at both ends by attachment to a centromere-like region parC, through a small DNA-binding protein ParR. Here, we present biochemical and electron microscopy data leading to a model for the mechanism by which ParR-parC complexes bind and stabilise elongating ParM filaments. We propose that the open ring formed by oligomeric ParR dimers with parC DNA wrapped around acts as a rigid clamp, which holds the end of elongating ParM filaments while allowing entry of new ATP-bound monomers. We propose a processive mechanism by which cycles of ATP hydrolysis in polymerising ParM drives movement of ParR-bound parC DNA. Importantly, our model predicts that each pair of plasmids will be driven apart in the cell by just a single double helical ParM filament.
机译:R1质粒雇佣了ATP-driven聚合actin-like蛋白质的改新细菌的DNA复制磁极细胞。准确的隔离low-copy号码质粒和特征是最好的例子在原核生物DNA分区。只有形式限制在两个时长的细丝目的通过附件centromere-like地区帕洛阿尔托研究中心,通过一个小帕尔dna结合蛋白质。在这里,我们目前的生化和电子显微镜数据模型ParR-parC复合物绑定和机制稳定延伸及ParM细丝。的开环形成的低聚物的帕尔二聚体与帕洛阿尔托研究中心DNA缠绕在充当刚性夹,延伸的结束改细丝,同时允许新条目ATP-bound单体。周期的ATP水解的机理聚合及ParM ParR-bound驱动器运动帕洛阿尔托研究中心的DNA。每一对的质粒在驱动细胞通过一个双重螺旋改灯丝。

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