ZMYND8 Co-localizes with NuRD on Target Genes and Regulates 
Poly(ADP-Ribose)-Dependent Recruitment of GATAD2A/NuRD to Sites of DNA Damage.

Spruijt, Cornelia G; Luijsterburg, Martijn S; Menafra, Roberta; Lindeboom, Rik G H; Jansen, Pascal W T C; Edupuganti, Raghu Ram; Baltissen, Marijke P; Wiegant, Wouter W; Voelker-Albert, Moritz C; Matarese, Filomena; Mensinga, Anneloes; Poser, Ina; Vos, Harmjan R; Stunnenberg, Hendrik G; Attikum, Haico van; Vermeulen, Michiel

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ZMYND8 Co-localizes with NuRD on Target Genes and Regulates Poly(ADP-Ribose)-Dependent Recruitment of GATAD2A/NuRD to Sites of DNA Damage.

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Poser, Ina
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

Stunnenberg, Hendrik G
Max Planck Society;

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Citation

Spruijt, C. G., Luijsterburg, M. S., Menafra, R., Lindeboom, R. G. H., Jansen, P. W. T. C., Edupuganti, R. R., et al. (2016). ZMYND8 Co-localizes with NuRD on Target Genes and Regulates Poly(ADP-Ribose)-Dependent Recruitment of GATAD2A/NuRD to Sites of DNA Damage. Cell Reports, 17(3), 783-798.

Cite as: https://hdl.handle.net/21.11116/0000-0001-03A5-1

Abstract

NuRD (nucleosome remodeling and histone deacetylase) is a versatile multi-protein complex with roles in transcription regulation and the DNA damage response. Here, we show that ZMYND8 bridges NuRD to a number of putative DNA-binding zinc finger proteins. The MYND domain of ZMYND8 directly interacts with PPPLΦ motifs in the NuRD subunit GATAD2A. Both GATAD2A and GATAD2B exclusively form homodimers and define mutually exclusive NuRD subcomplexes. ZMYND8 and NuRD share a large number of genome-wide binding sites, mostly active promoters and enhancers. Depletion of ZMYND8 does not affect NuRD occupancy genome-wide and only slightly affects expression of NuRD/ZMYND8 target genes. In contrast, the MYND domain in ZMYND8 facilitates the rapid, poly(ADP-ribose)-dependent recruitment of GATAD2A/NuRD to sites of DNA damage to promote repair by homologous recombination. Thus, these results show that a specific substoichiometric interaction with a NuRD subunit paralogue provides unique functionality to distinct NuRD subcomplexes.