Open AccessMultiple roles for PARP1 in ALC1-dependent nucleosome remodeling
Author(s) -
SoonKeat Ooi,
Shigeo Sato,
Chieri TomomoriSato,
Ying Zhang,
Zhihui Wen,
Charles A.S. Banks,
Michael P. Washburn,
Jay R. Unruh,
Laurence Florens,
Ronald Conaway,
Joan Conaway
Publication year - 2021
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2107277118
Subject(s) - chromatin remodeling , nucleosome , parp1 , chromatin structure remodeling (rsc) complex , chromatin , microbiology and biotechnology , biology , poly adp ribose polymerase , atpase , polymerase , biochemistry , chemistry , dna , enzyme
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.
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