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DOI | 10.1038/ncomms15414 |
RuvC uses dynamic probing of the Holliday junction to achieve sequence specificity and efficient resolution | |
Gorecka, Karolina Maria1; Krepl, Miroslav2; Szlachcic, Aleksandra1; Poznanski, Jaroslaw3; Sponer, Jiri2,4; Nowotny, Marcin1 | |
2019-09-10 | |
发表期刊 | NATURE COMMUNICATIONS |
ISSN | 2041-1723 |
出版年 | 2019 |
卷号 | 10 |
文章类型 | Article |
语种 | 英语 |
国家 | Poland; Czech Republic |
英文摘要 | Holliday junctions (HJs) are four-way DNA structures that occur in DNA repair by homologous recombination. Specialized nucleases, termed resolvases, remove (i.e., resolve) HJs. The bacterial protein RuvC is a canonical resolvase that introduces two symmetric cuts into the HJ. For complete resolution of the HJ, the two cuts need to be tightly coordinated. They are also specific for cognate DNA sequences. Using a combination of structural biology, biochemistry, and a computational approach, here we show that correct positioning of the substrate for cleavage requires conformational changes within the bound DNA. These changes involve rare high-energy states with protein-assisted base flipping that are readily accessible for the cognate DNA sequence but not for non-cognate sequences. These conformational changes and the relief of protein-induced structural tension of the DNA facilitate coordination between the two cuts. The unique DNA cleavage mechanism of RuvC demonstrates the importance of high-energy conformational states in nucleic acid readouts. |
领域 | 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000484992500001 |
WOS关键词 | RESOLVING ENZYME CCE1 ; ESCHERICHIA-COLI ; MOLECULAR-DYNAMICS ; CRYSTAL-STRUCTURES ; DNA JUNCTIONS ; MECHANISM ; CLEAVAGE ; PROTEIN ; COMPLEX ; BINDING |
WOS类目 | Multidisciplinary Sciences |
WOS研究方向 | Science & Technology - Other Topics |
URL | 查看原文 |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://119.78.100.173/C666/handle/2XK7JSWQ/203324 |
专题 | 资源环境科学 |
作者单位 | 1.Int Inst Mol & Cell Biol, Lab Prot Struct, 4 Trojdena St, PL-02109 Warsaw, Poland; 2.Czech Acad Sci, Inst Biophys, Kralovopolska 135, Brno 61265, Czech Republic; 3.Polish Acad Sci, Inst Biochem & Biophys, 5a Pawinskiego St, PL-02106 Warsaw, Poland; 4.Palacky Univ Olomouc, Reg Ctr Adv Technol & Mat, Fac Sci, Slechtitelu 27, Olomouc 77146, Czech Republic |
推荐引用方式 GB/T 7714 | Gorecka, Karolina Maria,Krepl, Miroslav,Szlachcic, Aleksandra,et al. RuvC uses dynamic probing of the Holliday junction to achieve sequence specificity and efficient resolution[J]. NATURE COMMUNICATIONS,2019,10. |
APA | Gorecka, Karolina Maria,Krepl, Miroslav,Szlachcic, Aleksandra,Poznanski, Jaroslaw,Sponer, Jiri,&Nowotny, Marcin.(2019).RuvC uses dynamic probing of the Holliday junction to achieve sequence specificity and efficient resolution.NATURE COMMUNICATIONS,10. |
MLA | Gorecka, Karolina Maria,et al."RuvC uses dynamic probing of the Holliday junction to achieve sequence specificity and efficient resolution".NATURE COMMUNICATIONS 10(2019). |
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