Gracheva, Ekaterina ; Chitale, Shalaka ; Wilhelm, Thomas ; Rapp, Alexander ; Byrne, Jonathan ; Stadler, Jens ; Medina, Rebeca ; Cardoso, M. Cristina ; Richly, Holger (2016)
ZRF1 mediates remodeling of E3 ligases at DNA lesion sites during nucleotide excision repair.
In: The Journal of cell biology, 213 (2)
Artikel, Bibliographie
Kurzbeschreibung (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.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2016 |
| Autor(en): | Gracheva, Ekaterina ; Chitale, Shalaka ; Wilhelm, Thomas ; Rapp, Alexander ; Byrne, Jonathan ; Stadler, Jens ; Medina, Rebeca ; Cardoso, M. Cristina ; Richly, Holger |
| Art des Eintrags: | Bibliographie |
| Titel: | ZRF1 mediates remodeling of E3 ligases at DNA lesion sites during nucleotide excision repair. |
| Sprache: | Englisch |
| Publikationsjahr: | 2016 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | The Journal of cell biology |
| Jahrgang/Volume einer Zeitschrift: | 213 |
| (Heft-)Nummer: | 2 |
| Kurzbeschreibung (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. |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie 10 Fachbereich Biologie > Cell Biology and Epigenetics |
| Hinterlegungsdatum: | 25 Apr 2016 12:23 |
| Letzte Änderung: | 28 Jun 2016 05:38 |
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