The structure and function of an RNA polymerase interaction domain in the PcrA/UvrD helicase.
The structure and function of an RNA polymerase interaction domain in the PcrA/UvrD helicase.
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DOI：
10.1093/nar/gkx074
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发表时间：
2017-04-20
影响因子：
14.9
通讯作者：
Dillingham MS
中科院分区：
文献类型：
--
作者：
Sanders K;Lin CL;Smith AJ;Cronin N;Fisher G;Eftychidis V;McGlynn P;Savery NJ;Wigley DB;Dillingham MS
PcrA/UvrD解旋酶在促进细菌基因组稳定性的多种途径中发挥作用，包括抑制复制和转录之间的冲突以及促进转录DNA的修复。报道的PcrA/UvrD结合和回溯RNA聚合酶的能力可能与这些功能有关，但这种活性的结构基础知之甚少。在这项工作中，我们定义了一个最小的RNA聚合酶的相互作用域在PcrA，并报告其晶体结构在1.5 μ m分辨率。该结构域采用类似于其他RNA聚合酶相互作用结构域的Tudor样折叠，包括原型转录修复偶联因子Mfd。去除或突变的相互作用结构域降低的能力PcrA/UvrD相互作用和重塑RNA聚合酶复合物在体外。这项工作的影响，我们了解的作用PcrA/UvrD在DNA复制，转录和修复的接口进行了讨论。
The PcrA/UvrD helicase functions in multiple pathways that promote bacterial genome stability including the suppression of conflicts between replication and transcription and facilitating the repair of transcribed DNA. The reported ability of PcrA/UvrD to bind and backtrack RNA polymerase might be relevant to these functions, but the structural basis for this activity is poorly understood. In this work, we define a minimal RNA polymerase interaction domain in PcrA, and report its crystal structure at 1.5 Å resolution. The domain adopts a Tudor-like fold that is similar to other RNA polymerase interaction domains, including that of the prototype transcription-repair coupling factor Mfd. Removal or mutation of the interaction domain reduces the ability of PcrA/UvrD to interact with and to remodel RNA polymerase complexes in vitro. The implications of this work for our understanding of the role of PcrA/UvrD at the interface of DNA replication, transcription and repair are discussed.