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Full-Text Articles in Medicine and Health Sciences
Hit And Run Versus Long-Term Activation Of Parp-1 By Its Different Domains Fine-Tunes Nuclear Processes., Colin Thomas, Md, Yingbiao Ji, Chao Wu, Haily Datz, Cody Boyle, Brett Macleod, Shri Patel, Michelle Ampofo, Michelle Currie, Jonathan Harbin, Kate Pechenkina, Niraj Lodhi, Sarah J. Johnson, Alexei V. Tulin
Hit And Run Versus Long-Term Activation Of Parp-1 By Its Different Domains Fine-Tunes Nuclear Processes., Colin Thomas, Md, Yingbiao Ji, Chao Wu, Haily Datz, Cody Boyle, Brett Macleod, Shri Patel, Michelle Ampofo, Michelle Currie, Jonathan Harbin, Kate Pechenkina, Niraj Lodhi, Sarah J. Johnson, Alexei V. Tulin
Department of Medicine Faculty Papers
Poly(ADP-ribose) polymerase 1 (PARP-1) is a multidomain multifunctional nuclear enzyme involved in the regulation of the chromatin structure and transcription. PARP-1 consists of three functional domains: the N-terminal DNA-binding domain (DBD) containing three zinc fingers, the automodification domain (A), and the C-terminal domain, which includes the protein interacting WGR domain (W) and the catalytic (Cat) subdomain responsible for the poly(ADP ribosyl)ating reaction. The mechanisms coordinating the functions of these domains and determining the positioning of PARP-1 in chromatin remain unknown. Using multiple deletional isoforms of PARP-1, lacking one or another of its three domains, as well as consisting of only …