Structural Basis for DNA Damage–Dependent Poly(ADP-ribosyl)ation by Human PARP-1

Author:

Langelier Marie-France1,Planck Jamie L.1,Roy Swati1,Pascal John M.1

Affiliation:

1. Department of Biochemistry and Molecular Biology, The Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA 19107, USA.

Abstract

Dissecting DNA Repair Covalent modification of proteins can be a crucial regulatory event. Poly(ADP-ribose) polymerase 1 (PARP-1) (ADP, adenosine diphosphate) synthesizes poly(ADP-ribose), which is attached to and regulates proteins involved in DNA repair. Langelier et al. (p. 728 ; see the Perspective by Gagné et al. ) use x-ray crystallography and biochemical analysis to demonstrate how PARP-1 detects DNA damage and how the interaction with DNA is coupled to poly(ADP-ribosyl)ation activity.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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