Bridging of DNA breaks activates PARP2-HPF1 to modify chromatin.

ABSTRACT: Breaks in DNA strands recruit the protein PARP1 and its paralogue PARP2 to modify histones and other substrates through the addition of mono- and poly(ADP-ribose) (PAR)^1-5. In the DNA damage responses, this post-translational modification occurs predominantly on serine residues^6-8 and requires HPF1, an accessory factor that switches the amino acid specificity of PARP1 and PARP2 from aspartate or glutamate to serine^9,10. Poly(ADP) ribosylation (PARylation) is important for subsequent chromatin decompaction and provides an anchor for the recruitment of downstream signalling and repair factors to the sites of DNA breaks^2,11. Here, to understand the molecular mechanism by which PARP enzymes recognize DNA breaks within chromatin, we determined the cry

SUBMITTER: Bilokapic S 

PROVIDER: S-EPMC7529888 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature