A close look at PARP-1

Kirk, Rebecca

doi:10.1038/nrclinonc.2012.93

Research Highlight
Published: 29 May 2012

Basic research

A close look at PARP-1

Rebecca Kirk

Nature Reviews Clinical Oncology volume 9, page 369 (2012)Cite this article

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Structural biology is one of the few disciplines that really allow us to have a close look at what is going on when proteins and DNA interact. One such interaction that is of interest to cancer researchers and oncologists alike, is the binding of poly(ADP-ribose) polymerase (PARP-1) to DNA strand breaks. Researchers led by John Pascal have now solved the crystal structure of this complex to 3.25 Å resolution, and have cast light on how the catalytic domain of PARP-1 links with the DNA-damage interface.

The reason the PARP-1 structure is of such interest lies in the activity of the protein. PARP-1 is activated in response to DNA damage and is involved in the first step in a cascade of DNA strand break repair. As Pascal explains: “upon detecting DNA damage, PARP-1 creates the post-translational modification poly(ADP-ribose), which sets the stage for DNA repair and contributes to cell fate decisions in the face of genotoxic stress.”

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ORIGINAL RESEARCH PAPER

Langelier, M.-F. et al. Structural basis for DNA damage-dependent poly(ADP-ribosyl)ation by human PARP-1. Science doi:10.1126/science.1216338
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