Multiple roles for PARP1 in ALC1-dependent nucleosome remodeling.

Autor: Soon-Keat Ooi, Shigeo Sato, Chieri Tomomori-Sato, Ying Zhang, Zhihui Wen, Banks, Charles A. S., Washburn, Michael P., Unruh, Jay R., Florens, Laurence, Conaway, Ronald C., Conaway, Joan W.
Předmět:
Zdroj: Proceedings of the National Academy of Sciences of the United States of America; 9/7/2021, Vol. 118 Issue 36, p1-7, 7p
Abstrakt: The SNF2 family ATPase Amplified in Liver Cancer 1 (ALC1) is the only chromatin remodeling enzyme with a poly(ADP-ribose) (PAR) binding macrodomain. ALC1 functions together with poly(ADP-ribose) polymerase PARP1 to remodel nucleosomes. Activation of ALC1 cryptic ATPase activity and the subsequent nucleosome remodeling requires binding of its macrodomain to PAR chains synthesized by PARP1 and NAD+. A key question is whether PARP1 has a role(s) in ALC1-dependent nucleosome remodeling beyond simply synthesizing the PAR chains needed to activate the ALC1 ATPase. Here, we identify PARP1 separation-of-function mutants that activate ALC1 ATPase but do not support nucleosome remodeling by ALC1. Investigation of these mutants has revealed multiple functions for PARP1 in ALC1-dependent nucleosome remodeling and provides insights into its multifaceted role in chromatin remodeling. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index