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ZRF1 mediates remodeling of E3 ligases at DNA lesion sites during nucleotide excision repair.

Gracheva, Ekaterina and Chitale, Shalaka and Wilhelm, Thomas and Rapp, Alexander and Byrne, Jonathan and Stadler, Jens and Medina, Rebeca and Cardoso, M. Cristina and Richly, Holger :
ZRF1 mediates remodeling of E3 ligases at DNA lesion sites during nucleotide excision repair.
In: The Journal of cell biology, 213 (2) pp. 185-200. ISSN 1540-8140
[Article] , (2016)

Abstract

Faithful DNA repair is essential to maintain genome integrity. Ultraviolet (UV) irradiation elicits both the recruitment of DNA repair factors and the deposition of histone marks such as monoubiquitylation of histone H2A at lesion sites. Here, we report how a ubiquitin E3 ligase complex specific to DNA repair is remodeled at lesion sites in the global genome nucleotide excision repair (GG-NER) pathway. Monoubiquitylation of histone H2A (H2A-ubiquitin) is catalyzed predominantly by a novel E3 ligase complex consisting of DDB2, DDB1, CUL4B, and RING1B (UV-RING1B complex) that acts early during lesion recognition. The H2A-ubiquitin binding protein ZRF1 mediates remodeling of this E3 ligase complex directly at the DNA lesion site, causing the assembly of the UV-DDB-CUL4A E3 ligase complex (DDB1-DDB2-CUL4A-RBX1). ZRF1 is an essential factor in GG-NER, and its function at damaged chromatin sites is linked to damage recognition factor XPC. Overall, the results shed light on the interplay between epigenetic and DNA repair recognition factors at DNA lesion sites.

Item Type: Article
Erschienen: 2016
Creators: Gracheva, Ekaterina and Chitale, Shalaka and Wilhelm, Thomas and Rapp, Alexander and Byrne, Jonathan and Stadler, Jens and Medina, Rebeca and Cardoso, M. Cristina and Richly, Holger
Title: ZRF1 mediates remodeling of E3 ligases at DNA lesion sites during nucleotide excision repair.
Language: English
Abstract:

Faithful DNA repair is essential to maintain genome integrity. Ultraviolet (UV) irradiation elicits both the recruitment of DNA repair factors and the deposition of histone marks such as monoubiquitylation of histone H2A at lesion sites. Here, we report how a ubiquitin E3 ligase complex specific to DNA repair is remodeled at lesion sites in the global genome nucleotide excision repair (GG-NER) pathway. Monoubiquitylation of histone H2A (H2A-ubiquitin) is catalyzed predominantly by a novel E3 ligase complex consisting of DDB2, DDB1, CUL4B, and RING1B (UV-RING1B complex) that acts early during lesion recognition. The H2A-ubiquitin binding protein ZRF1 mediates remodeling of this E3 ligase complex directly at the DNA lesion site, causing the assembly of the UV-DDB-CUL4A E3 ligase complex (DDB1-DDB2-CUL4A-RBX1). ZRF1 is an essential factor in GG-NER, and its function at damaged chromatin sites is linked to damage recognition factor XPC. Overall, the results shed light on the interplay between epigenetic and DNA repair recognition factors at DNA lesion sites.

Journal or Publication Title: The Journal of cell biology
Volume: 213
Number: 2
Divisions: 10 Department of Biology
10 Department of Biology > Cell Biology and Epigenetics
Date Deposited: 25 Apr 2016 12:23
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