DICER and ZRF1 contribute to chromatin decondensation during nucleotide excision repair.
作者： Shalaka Chitale , Holger Richly
DOI: 10.1093/NAR/GKX261
关键词: Biology 、 Endonuclease 、 Ubiquitin 、 Chromatin 、 DNA repair 、 DNA 、 Chromatin remodeling 、 Nucleotide excision repair 、 Molecular biology 、 Dicer
摘要: Repair of damaged DNA relies on the recruitment repair factors in a well orchestrated manner. As prerequisite, chromatin needs to be decondensed by remodelers allow for binding and occur. Recent studies have implicated members SWI/SNF INO80 families as PARP1 nucleotide excision (NER). In this study, we report that endonuclease DICER is decondensation during NER. response UV irradiation, recruited ZRF1-mediated The H2A–ubiquitin protein ZRF1 together impact conformation via PARP1. Moreover, DICER-mediated independent its catalytic activity. Taken together, describe novel function at interaction with ubiquitin signalling cascade GG-NER.
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