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Related Concept Videos

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Organisms are capable of detecting and fixing nucleotide mismatches that occur during DNA replication. This sophisticated process requires identifying the new strand and replacing the erroneous bases with correct nucleotides. Mismatch repair is coordinated by many proteins in both prokaryotes and eukaryotes.
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Using Next Generation Sequencing to Identify Mutations Associated with Repair of a CAS9-induced Double Strand Break Near the CD4 Promoter
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Structural step forward for NHEJ.

Go Watanabe1, Michael R Lieber1, Dewight Williams2

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|September 20, 2017
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Summary
This summary is machine-generated.

A new cryo-EM structure shows how DNA-PKcs and Ku70/80:DNA interact to regulate DNA repair. This reveals the mechanism of kinase activity in the DNA-dependent protein kinase holoenzyme.

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Area of Science:

  • Structural Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Non-homologous DNA end joining (NHEJ) is a critical DNA repair pathway.
  • The DNA-dependent protein kinase (DNA-PK) holoenzyme, comprising DNA-PKcs and Ku70/80:DNA, is central to NHEJ.
  • Understanding the regulation of DNA-PKcs activity is key to comprehending DNA repair fidelity.

Purpose of the Study:

  • To elucidate the structural basis of DNA-PK holoenzyme assembly.
  • To reveal the mechanism by which Ku70/80:DNA binding regulates DNA-PKcs kinase activity.
  • To provide insights into the allosteric control of DNA-PKcs within the phosphoinositide 3-kinase-related kinase family.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was employed to determine the high-resolution structure of the DNA-PK holoenzyme.
  • Structural analysis focused on the interface between DNA-PKcs and the Ku70/80:DNA complex.
  • Biochemical assays were used to assess kinase activity regulation.

Main Results:

  • The cryo-EM structure reveals the precise interface between DNA-PKcs and the Ku70/80:DNA complex.
  • The structure suggests an allosteric rearrangement of DNA-PKcs upon binding to Ku70/80:DNA.
  • This rearrangement is proposed to be the mechanism regulating DNA-PKcs kinase activity.

Conclusions:

  • The determined structure provides a mechanistic understanding of DNA-PK holoenzyme assembly and regulation.
  • The findings highlight the role of allosteric control in modulating kinase activity within this crucial DNA repair complex.
  • This work deepens our knowledge of DNA repair pathways and the broader family of phosphoinositide 3-kinase-related kinases.