CHD1L
Domain
The macro domain mediates non-covalent poly(ADP-ribose)-binding and recruitment to DNA damage sites (PubMed:19661379, PubMed:29220652, PubMed:29220653). Mediates auto-inhibition of ATPase activity by interacting with the N-terminal ATPase module, encompassing the helicase ATP-binding domain and helicase C-terminal domain (PubMed:29220652, PubMed:29220653). Binding to poly-ADP-ribosylated histones upon DNA damage releases the auto-inhibition by the macro domain and trigger ATPase activity (PubMed:34486521, PubMed:34874266). Does not bind monomeric ADP-ribose and mono-ADP-ribose fails to release the auto-inhibition of the ATPase module by the macro domain (PubMed:29220653).
Function
ATP-dependent chromatin remodeler that mediates chromatin-remodeling following DNA damage (PubMed:19661379, PubMed:29220652, PubMed:29220653, PubMed:33357431, PubMed:34210977, PubMed:34486521, PubMed:34874266). Recruited to DNA damage sites through interaction with poly-ADP-ribose: specifically recognizes and binds histones that are poly-ADP-ribosylated on serine residues in response to DNA damage (PubMed:19661379, PubMed:29220652, PubMed:29220653, PubMed:34486521, PubMed:34874266). Poly-ADP-ribose-binding activates the ATP-dependent chromatin remodeler activity, thereby regulating chromatin during DNA repair (PubMed:19661379, PubMed:29220652, PubMed:29220653, PubMed:34486521, PubMed:34874266). Catalyzes nucleosome sliding away from DNA breaks in an ATP-dependent manner (PubMed:19661379, PubMed:29220652, PubMed:29220653). Chromatin remodeling activity promotes PARP2 removal from chromatin (PubMed:33275888).
Sequence Similarities
Belongs to the SNF2/RAD54 helicase family.
Tissue Specificity
Frequently overexpressed in hepatomacellular carcinomas.
Cellular localization
- Nucleus
- Chromosome
- Localizes at sites of DNA damage; recruited by histones H2B and H3 poly-ADP-ribosylated on 'Ser-6' and 'Ser-10', respectively (H2BS6ADPr and H3S10ADPr) by PARP1 or PARP2.
Alternative names
ALC1, CHD1L, Chromodomain-helicase-DNA-binding protein 1-like, Amplified in liver cancer protein 1