DICER and ZRF1 contribute to chromatin decondensation during nucleotide excision repair.
Repair of damaged DNA relies on the recruitment of DNA repair factors in a well orchestrated manner. As a prerequisite, the chromatin needs to be decondensed by chromatin remodelers to allow for binding of repair factors and for DNA repair to occur. Recent studies have implicated members of the SWI/SNF ... and INO80 families as well as PARP1 in nucleotide excision repair (NER). In this study, we report that the endonuclease DICER is implicated in chromatin decondensation during NER. In response to UV irradiation, DICER is recruited to chromatin in a ZRF1-mediated manner. The H2A-ubiquitin binding protein ZRF1 and DICER together impact on the chromatin conformation via PARP1. Moreover, DICER-mediated chromatin decondensation is independent of its catalytic activity. Taken together, we describe a novel function of DICER at chromatin and its interaction with the ubiquitin signalling cascade during GG-NER.
Mesh Terms:
Animals, Caenorhabditis elegans, Cell Line, Cell Line, Tumor, Chromatin, Chromatin Assembly and Disassembly, DEAD-box RNA Helicases, DNA Damage, DNA Repair, DNA-Binding Proteins, Fibroblasts, HEK293 Cells, Histones, Humans, Molecular Chaperones, Oncogene Proteins, Osteoblasts, Poly (ADP-Ribose) Polymerase-1, RNA-Binding Proteins, Ribonuclease III, Ubiquitin, Ultraviolet Rays
Animals, Caenorhabditis elegans, Cell Line, Cell Line, Tumor, Chromatin, Chromatin Assembly and Disassembly, DEAD-box RNA Helicases, DNA Damage, DNA Repair, DNA-Binding Proteins, Fibroblasts, HEK293 Cells, Histones, Humans, Molecular Chaperones, Oncogene Proteins, Osteoblasts, Poly (ADP-Ribose) Polymerase-1, RNA-Binding Proteins, Ribonuclease III, Ubiquitin, Ultraviolet Rays
Nucleic Acids Res
Date: Jun. 02, 2017
PubMed ID: 28402505
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