@article{
 title = {The Nucleosome Remodeling and Deacetylase Complex Has an Asymmetric, Dynamic, and Modular Architecture},
 type = {article},
 year = {2020},
 volume = {33},
 id = {a494d066-7bf4-3d91-b39e-2c81a3c17fb6},
 created = {2023-01-10T01:44:03.714Z},
 file_attached = {false},
 profile_id = {a5a2ab6f-a8b5-3db6-97bc-618752ee4386},
 group_id = {bc1ab1d4-9e57-37e6-9fb5-435fca0ee9d2},
 last_modified = {2023-01-10T01:44:03.714Z},
 read = {false},
 starred = {false},
 authored = {false},
 confirmed = {false},
 hidden = {false},
 private_publication = {false},
 abstract = {Low et al. examine the architecture of the nucleosome remodeling and deacetylase complex. They define its stoichiometry, use cross-linking mass spectrometry to define subunit locations, and use electron microscopy to reveal large-scale dynamics. They also demonstrate that PWWP2A competes with MBD3 to sequester the HDAC-MTA-RBBP module from NuRD.SCOPUS_ABS_SEPARATORThe nucleosome remodeling and deacetylase (NuRD) complex is essential for metazoan development but has been refractory to biochemical analysis. We present an integrated analysis of the native mammalian NuRD complex, combining quantitative mass spectrometry, cross-linking, protein biochemistry, and electron microscopy to define the architecture of the complex. NuRD is built from a 2:2:4 (MTA, HDAC, and RBBP) deacetylase module and a 1:1:1 (MBD, GATAD2, and Chromodomain-Helicase-DNA-binding [CHD]) remodeling module, and the complex displays considerable structural dynamics. The enigmatic GATAD2 controls the asymmetry of the complex and directly recruits the CHD remodeler. The MTA-MBD interaction acts as a point of functional switching, with the transcriptional regulator PWWP2A competing with MBD for binding to the MTA-HDAC-RBBP subcomplex. Overall, our data address the long-running controversy over NuRD stoichiometry, provide imaging of the mammalian NuRD complex, and establish the biochemical mechanism by which PWWP2A can regulate NuRD composition.},
 bibtype = {article},
 author = {Low, J.K.K. and Silva, A.P.G. and Sharifi Tabar, M. and Torrado, M. and Webb, S.R. and Parker, B.L. and Sana, M. and Smits, C. and Schmidberger, J.W. and Brillault, L. and Landsberg, M.J. and Mackay, J.P.},
 doi = {10.1016/j.celrep.2020.108450},
 journal = {Cell Reports},
 number = {9}
}

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They define its stoichiometry, use cross-linking mass spectrometry to define subunit locations, and use electron microscopy to reveal large-scale dynamics. They also demonstrate that PWWP2A competes with MBD3 to sequester the HDAC-MTA-RBBP module from NuRD.SCOPUS_ABS_SEPARATORThe nucleosome remodeling and deacetylase (NuRD) complex is essential for metazoan development but has been refractory to biochemical analysis. We present an integrated analysis of the native mammalian NuRD complex, combining quantitative mass spectrometry, cross-linking, protein biochemistry, and electron microscopy to define the architecture of the complex. NuRD is built from a 2:2:4 (MTA, HDAC, and RBBP) deacetylase module and a 1:1:1 (MBD, GATAD2, and Chromodomain-Helicase-DNA-binding [CHD]) remodeling module, and the complex displays considerable structural dynamics. The enigmatic GATAD2 controls the asymmetry of the complex and directly recruits the CHD remodeler. The MTA-MBD interaction acts as a point of functional switching, with the transcriptional regulator PWWP2A competing with MBD for binding to the MTA-HDAC-RBBP subcomplex. Overall, our data address the long-running controversy over NuRD stoichiometry, provide imaging of the mammalian NuRD complex, and establish the biochemical mechanism by which PWWP2A can regulate NuRD composition.","bibtype":"article","author":"Low, J.K.K. and Silva, A.P.G. and Sharifi Tabar, M. and Torrado, M. and Webb, S.R. and Parker, B.L. and Sana, M. and Smits, C. and Schmidberger, J.W. and Brillault, L. and Landsberg, M.J. and Mackay, J.P.","doi":"10.1016/j.celrep.2020.108450","journal":"Cell Reports","number":"9","bibtex":"@article{\n title = {The Nucleosome Remodeling and Deacetylase Complex Has an Asymmetric, Dynamic, and Modular Architecture},\n type = {article},\n year = {2020},\n volume = {33},\n id = {a494d066-7bf4-3d91-b39e-2c81a3c17fb6},\n created = {2023-01-10T01:44:03.714Z},\n file_attached = {false},\n profile_id = {a5a2ab6f-a8b5-3db6-97bc-618752ee4386},\n group_id = {bc1ab1d4-9e57-37e6-9fb5-435fca0ee9d2},\n last_modified = {2023-01-10T01:44:03.714Z},\n read = {false},\n starred = {false},\n authored = {false},\n confirmed = {false},\n hidden = {false},\n private_publication = {false},\n abstract = {Low et al. examine the architecture of the nucleosome remodeling and deacetylase complex. They define its stoichiometry, use cross-linking mass spectrometry to define subunit locations, and use electron microscopy to reveal large-scale dynamics. They also demonstrate that PWWP2A competes with MBD3 to sequester the HDAC-MTA-RBBP module from NuRD.SCOPUS_ABS_SEPARATORThe nucleosome remodeling and deacetylase (NuRD) complex is essential for metazoan development but has been refractory to biochemical analysis. We present an integrated analysis of the native mammalian NuRD complex, combining quantitative mass spectrometry, cross-linking, protein biochemistry, and electron microscopy to define the architecture of the complex. NuRD is built from a 2:2:4 (MTA, HDAC, and RBBP) deacetylase module and a 1:1:1 (MBD, GATAD2, and Chromodomain-Helicase-DNA-binding [CHD]) remodeling module, and the complex displays considerable structural dynamics. The enigmatic GATAD2 controls the asymmetry of the complex and directly recruits the CHD remodeler. The MTA-MBD interaction acts as a point of functional switching, with the transcriptional regulator PWWP2A competing with MBD for binding to the MTA-HDAC-RBBP subcomplex. 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