The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding.

The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding.
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DOI:
10.1038/s41467-021-25429-2
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发表时间:
2021-08-27
影响因子:
16.6
通讯作者:
Bergeron JRC
Bergeron JRC
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Parker AV;Mann D;Tzokov SB;Hwang LC;Bergeron JRC

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复制遗传物质的有效分离是细胞分裂的关键步骤。细菌细胞使用几种进化上截然不同的基因组分离系统,其中最常见的是I型PAR系统。它包括一个适配蛋白PARB,它通过与Pars DNA序列的相互作用与DNA货物结合;以及一个ATPase,Para,它与非特异性DNA结合,并介导货物运输。然而,这个系统如何运作的分子细节还没有被很好地理解。在这里,我们报道了霍乱弧菌ParA2细丝与DNA结合的冷冻EM结构,以及该蛋白在不同核苷酸状态下的晶体结构。这些结构表明,Para在DNA上形成一个由核苷酸结合稳定的左手微丝,并在DNA结合和微丝组装时经历深刻的结构重排。总体而言,我们的数据表明了parA与DNA合作结合的结构基础,以及在类核上形成高para密度区域的结构基础。PARA是一种ATPase,参与细菌中新复制DNA的分离。在这里,对位细丝与DNA结合的结构和对位素在不同核苷酸状态下的结构提供了对其在DNA结合和细丝组装时的构象变化的洞察,包括对位素位与DNA协同结合的基础。
The efficient segregation of replicated genetic material is an essential step for cell division. Bacterial cells use several evolutionarily-distinct genome segregation systems, the most common of which is the type I Par system. It consists of an adapter protein, ParB, that binds to the DNA cargo via interaction with the parS DNA sequence; and an ATPase, ParA, that binds nonspecific DNA and mediates cargo transport. However, the molecular details of how this system functions are not well understood. Here, we report the cryo-EM structure of the Vibrio cholerae ParA2 filament bound to DNA, as well as the crystal structures of this protein in various nucleotide states. These structures show that ParA forms a left-handed filament on DNA, stabilized by nucleotide binding, and that ParA undergoes profound structural rearrangements upon DNA binding and filament assembly. Collectively, our data suggest the structural basis for ParA’s cooperative binding to DNA and the formation of high ParA density regions on the nucleoid. ParA is an ATPase involved in the segregation of newly replicated DNA in bacteria. Here, structures of a ParA filament bound to DNA and of ParA in various nucleotide states offer insight into its conformational changes upon DNA binding and filament assembly, including the basis for ParA’s cooperative binding to DNA.
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影响因子: 3.6
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