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- W2920599794 abstract "The nucleosome remodelling and deacetylase complex (NuRD) is a widely conserved regulator of gene expression. The determination of the subunit composition of the complex and identification of its binding partners are important steps towards understanding its architecture and function. The question of how these properties of the complex vary across different cell types has not been addressed in detail to date. Here, we set up a two-step purification protocol coupled to liquid chromatography-tandem mass spectrometry to assess NuRD composition and interaction partners in three different cancer cell lines, using label-free intensity-based absolute quantification (iBAQ). Our data indicate that the stoichiometry of the NuRD complex is preserved across our three different cancer cell lines. In addition, our interactome data suggest ZNF219 and SLC25A5 as possible interaction partners of the complex. To corroborate this latter finding, in vitro and cell-based pull-down experiments were carried out. These experiments indicated that ZNF219 can interact with RBBP4, GATAD2A/B and chromodomain helicase DNA binding 4, whereas SLC25A5 might interact with MTA2 and GATAD2A." @default.
- W2920599794 created "2019-03-11" @default.
- W2920599794 creator A5020208790 @default.
- W2920599794 creator A5053840975 @default.
- W2920599794 creator A5074575943 @default.
- W2920599794 date "2019-03-19" @default.
- W2920599794 modified "2023-10-16" @default.
- W2920599794 title "The stoichiometry and interactome of the Nucleosome Remodeling and Deacetylase (NuRD) complex are conserved across multiple cell lines" @default.
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- W2920599794 doi "https://doi.org/10.1111/febs.14800" @default.
- W2920599794 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30828972" @default.
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