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2
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本文引用的文献

1
Mechanisms of bacterial DNA replication restart.细菌 DNA 复制重启动的机制。
Nucleic Acids Res. 2018 Jan 25;46(2):504-519. doi: 10.1093/nar/gkx1203.
2
Transcription leads to pervasive replisome instability in bacteria.转录会导致细菌中普遍存在的复制体不稳定性。
Elife. 2017 Jan 16;6:e19848. doi: 10.7554/eLife.19848.
3
An aromatic-rich loop couples DNA binding and ATP hydrolysis in the PriA DNA helicase.富含芳香族氨基酸的环将PriA DNA解旋酶中的DNA结合与ATP水解偶联起来。
Nucleic Acids Res. 2016 Nov 16;44(20):9745-9757. doi: 10.1093/nar/gkw690. Epub 2016 Aug 2.
4
RecG Directs DNA Synthesis during Double-Strand Break Repair.RecG在双链断裂修复过程中指导DNA合成。
PLoS Genet. 2016 Feb 12;12(2):e1005799. doi: 10.1371/journal.pgen.1005799. eCollection 2016 Feb.
5
Crosslink Mapping at Amino Acid-Base Resolution Reveals the Path of Scrunched DNA in Initial Transcribing Complexes.氨基酸-碱基分辨率下的交联图谱揭示了初始转录复合物中压缩DNA的路径。
Mol Cell. 2015 Sep 3;59(5):768-80. doi: 10.1016/j.molcel.2015.06.037. Epub 2015 Aug 6.
6
HLTF's Ancient HIRAN Domain Binds 3' DNA Ends to Drive Replication Fork Reversal.HLTF的古老HIRAN结构域结合3'端DNA以驱动复制叉逆转。
Mol Cell. 2015 Jun 18;58(6):1090-100. doi: 10.1016/j.molcel.2015.05.013. Epub 2015 Jun 4.
7
Structural mechanisms of DNA binding and unwinding in bacterial RecQ helicases.细菌RecQ解旋酶中DNA结合与解旋的结构机制。
Proc Natl Acad Sci U S A. 2015 Apr 7;112(14):4292-7. doi: 10.1073/pnas.1416746112. Epub 2015 Mar 23.
8
Identification of Subunit Binding Positions on a Model Fork and Displacements That Occur during Sequential Assembly of the Escherichia coli Primosome.大肠杆菌引发体顺序组装过程中模型叉上亚基结合位置的鉴定及发生的位移
J Biol Chem. 2015 Apr 24;290(17):10828-39. doi: 10.1074/jbc.M115.642066. Epub 2015 Mar 5.
9
Structural mechanisms of PriA-mediated DNA replication restart.PriA 介导的 DNA 复制重启动的结构机制。
Proc Natl Acad Sci U S A. 2014 Jan 28;111(4):1373-8. doi: 10.1073/pnas.1318001111. Epub 2013 Dec 30.
10
Specificity in suppression of SOS expression by recA4162 and uvrD303.RecA4162 和 uvrD303 对 SOS 表达的抑制特异性。
DNA Repair (Amst). 2013 Dec;12(12):1072-80. doi: 10.1016/j.dnarep.2013.09.003. Epub 2013 Sep 29.

结构特异性 DNA 复制叉识别指导 PriA 解旋酶的解旋酶和复制重启动活性。

Structure-specific DNA replication-fork recognition directs helicase and replication restart activities of the PriA helicase.

机构信息

Department of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, WI 53706.

Department of Microbiology, University of Massachusetts Amherst, Amherst, MA 01003.

出版信息

Proc Natl Acad Sci U S A. 2018 Sep 25;115(39):E9075-E9084. doi: 10.1073/pnas.1809842115. Epub 2018 Sep 10.

DOI:10.1073/pnas.1809842115
PMID:30201718
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6166810/
Abstract

DNA replication restart, the essential process that reinitiates prematurely terminated genome replication reactions, relies on exquisitely specific recognition of abandoned DNA replication-fork structures. The PriA DNA helicase mediates this process in bacteria through mechanisms that remain poorly defined. We report the crystal structure of a PriA/replication-fork complex, which resolves leading-strand duplex DNA bound to the protein. Interaction with PriA unpairs one end of the DNA and sequesters the 3'-most nucleotide from the nascent leading strand into a conserved protein pocket. Cross-linking studies reveal a surface on the winged-helix domain of PriA that binds to parental duplex DNA. Deleting the winged-helix domain alters PriA's structure-specific DNA unwinding properties and impairs its activity in vivo. Our observations lead to a model in which coordinated parental-, leading-, and lagging-strand DNA binding provide PriA with the structural specificity needed to act on abandoned DNA replication forks.

摘要

DNA 复制重启动是一个关键的过程，它重新启动过早终止的基因组复制反应，依赖于对废弃的 DNA 复制叉结构的高度特异性识别。PriA DNA 解旋酶通过仍然定义不明确的机制在细菌中介导这个过程。我们报告了 PriA/复制叉复合物的晶体结构，该结构解析了与蛋白质结合的领头链双链 DNA。与 PriA 的相互作用使 DNA 的一端解配对，并将 3'-最核苷酸从新生的领头链隔离到保守的蛋白质口袋中。交联研究揭示了 PriA 的翼型螺旋结构域上与亲本双链 DNA 结合的一个表面。删除翼型螺旋结构域会改变 PriA 的结构特异性 DNA 解旋特性，并损害其在体内的活性。我们的观察结果提出了一个模型，即协调的亲本链、领头链和滞后链 DNA 结合为 PriA 提供了在废弃的 DNA 复制叉上发挥作用所需的结构特异性。