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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 act...

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Bibliographic Details
Published in:BioEssays 2016-11, Vol.38 (11), p.1130-1140
Main Authors: Papadopoulou, Thaleia, Richly, Holger
Format: Article
Language:English
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Summary: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. Remodeling of multiprotein complexes has emerged as a new concept of timing signaling processes at chromatin. Here we review the function of the H2A‐ubiquitin binding protein ZRF1 in multiprotein complex remodeling. ZRF1 operates as an adaptor protein presumably in conjunction with remodeling machines to modify the subunit composition of protein complexes.
ISSN:0265-9247
1521-1878
DOI:10.1002/bies.201600094