title: DICER and ZRF1 contribute to chromatin decondensation during nucleotide excision repair.
abstract: 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.
authors.affiliation: Laboratory of Molecular Epigenetics, Institute of Molecular Biology (IMB), Ackermannweg 4, 55128 Mainz, Germany.|Faculty of Biology, Johannes Gutenberg University, 55099 Mainz, Germany.
authors.forename: Shalaka
authors.initials: S
authors.lastname: Chitale
authors.affiliation: Laboratory of Molecular Epigenetics, Institute of Molecular Biology (IMB), Ackermannweg 4, 55128 Mainz, Germany.
authors.forename: Holger
authors.initials: H
authors.lastname: Richly
mesh_terms: D000818:Animals; D017173:Caenorhabditis elegans / Q000235:genetics* / Q000254:growth & development / Q000378:metabolism / Q000528:radiation effects; D002460:Cell Line; D045744:Cell Line, Tumor; D002843:Chromatin / Q000737:chemistry* / Q000378:metabolism; D042002:Chromatin Assembly and Disassembly; D053487:DEAD-box RNA Helicases / Q000235:genetics* / Q000378:metabolism; D004249:DNA Damage; D004260:DNA Repair; D004268:DNA-Binding Proteins / Q000235:genetics* / Q000378:metabolism; D005347:Fibroblasts / Q000166:cytology / Q000378:metabolism / Q000528:radiation effects; D057809:HEK293 Cells; D006657:Histones / Q000235:genetics / Q000378:metabolism; D006801:Humans; D018832:Molecular Chaperones; D015513:Oncogene Proteins / Q000235:genetics* / Q000378:metabolism; D010006:Osteoblasts / Q000166:cytology / Q000378:metabolism / Q000528:radiation effects; D000071137:Poly (ADP-Ribose) Polymerase-1 / Q000235:genetics / Q000378:metabolism; D016601:RNA-Binding Proteins; D043244:Ribonuclease III / Q000235:genetics* / Q000378:metabolism; D025801:Ubiquitin / Q000235:genetics / Q000378:metabolism; D014466:Ultraviolet Rays
chemical_list: D002843:Chromatin; D004268:DNA-Binding Proteins; C414672:DNAJC2 protein, human; D006657:Histones; D018832:Molecular Chaperones; D015513:Oncogene Proteins; D016601:RNA-Binding Proteins; D025801:Ubiquitin; C499320:PARP1 protein, human; D000071137:Poly (ADP-Ribose) Polymerase-1; C408087:DICER1 protein, human; D043244:Ribonuclease III; D053487:DEAD-box RNA Helicases