On-site remodeling at chromatin: How multiprotein complexes are rebuilt during DNA repair and transcriptional activation.
In this review, we discuss a novel on-site remodeling function that is mediated by the H2A-ubiquitin binding protein ZRF1. ZRF1 facilitates the remodeling of multiprotein complexes at chromatin and lies at the heart of signaling processes that occur at DNA damage sites and during transcriptional activation. In nucleotide excision repair ZRF1 remodels E3 ubiquitin ligase complexes at the damage site. During embryonic stem cell differentiation, it contributes to retinoic acid-mediated gene activation by altering the subunit composition of the Mediator complex. We postulate that ZRF1 operates in conjunction with cellular remodeling machines and suggest that on-site remodeling might be a hallmark of many chromatin-associated signaling pathways. We discuss yet unexplored functions of ZRF1-mediated remodeling in replication and double strand break repair. In conclusion, we postulate that on-site remodeling of multiprotein complexes is essential for the timing of chromatin signaling processes.
Laboratory of Molecular Epigenetics, Institute of Molecular Biology (IMB), Mainz, Germany.
Thaleia
T
Papadopoulou
Laboratory of Molecular Epigenetics, Institute of Molecular Biology (IMB), Mainz, Germany. h.richly@imb-mainz.de.
Holger
H
Richly
D000818:Animals; D042002:Chromatin Assembly and Disassembly; D004260:DNA Repair; D004268:DNA-Binding Proteins / Q000378:metabolism*; D006801:Humans; D018832:Molecular Chaperones; D046912:Multiprotein Complexes / Q000378:metabolism; D015513:Oncogene Proteins / Q000378:metabolism*; D016601:RNA-Binding Proteins; D015533:Transcriptional Activation
D004268:DNA-Binding Proteins; C414672:DNAJC2 protein, human; D018832:Molecular Chaperones; D046912:Multiprotein Complexes; D015513:Oncogene Proteins; D016601:RNA-Binding Proteins
DNA repair; Mediator; PRC1; ZRF1; transcription; ubiquitin