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Structural basis for DNA break recognition by ARTD2/PARP2.

Ezeogo Obaji1, Teemu Haikarainen1, Lari Lehtiö1

  • 1Faculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, Oulu, Finland.

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|October 16, 2018
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Summary
This summary is machine-generated.

Human ARTD2 (ARTD2) binds damaged DNA via its WGR domain, initiating DNA repair. Crystal structures reveal ARTD2 recognizes DNA breaks and can join DNA ends, highlighting the WGR domain

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Analysis of DNA Double-strand Break DSB Repair in Mammalian Cells
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Human ARTD2 (ARTD2), also known as PARP2, is an ADP-ribosyltransferase crucial for DNA repair.
  • Unlike ARTD1, ARTD2 lacks specialized zinc-fingers for DNA damage detection.
  • The precise mechanism of ARTD2's DNA damage recognition and activation remains unclear.

Purpose of the Study:

  • To elucidate the mechanism of DNA damage detection by ARTD2.
  • To determine the role of the ARTD2 WGR domain in DNA binding and activation.
  • To provide structural insights into ARTD2-DNA interactions.

Main Methods:

  • X-ray crystallography of the ARTD2 WGR domain bound to DNA oligonucleotides.
  • Site-directed mutagenesis of the ARTD2-DNA interface.
  • In vitro activity, binding, and stoichiometry assays.

Main Results:

  • Crystal structures reveal ARTD2 WGR domain binding to DNA ends through end-to-end interaction.
  • ARTD2 recognizes nicked DNA and interacts with the 5'-phosphate group.
  • The WGR domain is essential for DNA break detection, and ARTD2 can mediate DNA end joining in vitro.

Conclusions:

  • The ARTD2 WGR domain is the primary determinant for detecting DNA breaks.
  • Structural and biochemical data provide a mechanistic understanding of ARTD2's role in DNA repair initiation.
  • ARTD2's ability to mediate DNA end joining suggests a broader role in DNA repair pathways.