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TitleMechanisms of helicase activated DNA end resection in bacteria.
Journal, issue, pagesStructure, Vol. 30, Issue 9, Page 1298-11306.e3, Year 2022
Publish dateSep 1, 2022
AuthorsYing Xu / Lingyi Xu / Chen Qin / Liangyan Wang / Jiangtao Guo / Yuejin Hua / Ye Zhao /
PubMed AbstractDNA end resection mediated by the coordinated action of nuclease and helicase is a crucial step in initiating homologous recombination. The end-resection apparatus NurA nuclease and HerA helicase are ...DNA end resection mediated by the coordinated action of nuclease and helicase is a crucial step in initiating homologous recombination. The end-resection apparatus NurA nuclease and HerA helicase are present in both archaea and bacteria. Here, we report the cryo-electron microscopy structure of a bacterial HerA-NurA complex from Deinococcus radiodurans. The structure reveals a barrel-like hexameric HerA and a distinctive NurA dimer subcomplex, which has a unique extended N-terminal region (ENR) involved in bacterial NurA dimerization and activation. In addition to the long protruding linking loop and the C-terminal α helix of NurA, the flexible ENR is close to the HerA-NurA interface and divides the central channel of the DrNurA dimer into two halves, suggesting a possible mechanism of DNA end processing. In summary, this work provides new insights into the structure, assembly, and activation mechanisms of bacterial DNA end resection mediated by a minimal end-resection apparatus.
External linksStructure / PubMed:35841886
MethodsEM (single particle)
Resolution3.85 Å
Structure data

31478

7f6d

EMDB-31478, PDB-7f6d:
Reconstruction of the HerA-NurA complex from Deinococcus radiodurans
Method: EM (single particle) / Resolution: 3.85 Å

Source
  • deinococcus radiodurans r1 (radioresistant)
KeywordsHYDROLASE / nuclease / helicase / end resection / DNA repair

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