The Nucleosome Remodeling and Deacetylase complex has an asymmetric, dynamic, and modular architecture Article Swipe

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Jason K. K. Low , Ana PG Silva , Mehdi Sharifi Tabar , Mario Torrado , Sarah R. Webb , Benjamin L. Parker , Maryam Sana , C. Smits , Jason W. Schmidberger , Lou Brillault , Matthew J. Jackman , David Williams , Gerd A. Blobel , Sandra B. Hake , Nicholas E. Shepherd , Michael J. Landsberg , Joel P. Mackay ·

YOU? · · 2020 · Open Access · · DOI: https://doi.org/10.1101/2020.02.17.951822

The Nucleosome Remodeling and Deacetylase (NuRD) complex is essential for development in complex animals but has been refractory to biochemical analysis. We present the first integrated analysis of the architecture of the native mammalian NuRD complex, combining quantitative mass spectrometry, covalent cross-linking, protein biochemistry and electron microscopy. NuRD is built around a 2:2:4 pseudo-symmetric deacetylase module comprising MTA, HDAC and RBBP subunits. This module interacts asymmetrically with a remodeling module comprising one copy each of MBD, GATAD2 and CHD subunits. The previously enigmatic GATAD2 controls the asymmetry of the complex and directly recruits the ATP-dependent CHD remodeler. Unexpectedly, the MTA-MBD interaction acts as a point of functional switching. The transcriptional regulator PWWP2A modulates NuRD assembly by competing directly with MBD for binding to the MTA-HDAC-RBBP subcomplex, forming a ‘moonlighting’ PWWP2A-MTA-HDAC-RBBP complex that likely directs deacetylase activity to PWWP2A target sites. Taken together, our data describe the overall architecture of the intact NuRD complex and reveal aspects of its structural dynamics and functional plasticity.

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Computational Biology

Biochemistry

Dna

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Histone deacetylase Nucleosome Cell biology Acetylation Biology Histone Chemistry Computational biology Biochemistry DNA Gene

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Type: preprint
Language: en
Landing Page: https://doi.org/10.1101/2020.02.17.951822
PDF: https://www.biorxiv.org/content/biorxiv/early/2020/02/17/2020.02.17.951822.full.pdf
OA Status: green
Cited By: 6
References: 65
Related Works: 10
OpenAlex ID: https://openalex.org/W3006501733

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DOI: https://doi.org/10.1101/2020.02.17.951822

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Title: The Nucleosome Remodeling and Deacetylase complex has an asymmetric, dynamic, and modular architecture

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Type: preprint

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Language: en

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Publication year: 2020

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Publication date: 2020-02-17

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Authors: Jason K. K. Low, Ana PG Silva, Mehdi Sharifi Tabar, Mario Torrado, Sarah R. Webb, Benjamin L. Parker, Maryam Sana, C. Smits, Jason W. Schmidberger, Lou Brillault, Matthew J. Jackman, David Williams, Gerd A. Blobel, Sandra B. Hake, Nicholas E. Shepherd, Michael J. Landsberg, Joel P. Mackay

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Landing page: https://doi.org/10.1101/2020.02.17.951822

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PDF URL: https://www.biorxiv.org/content/biorxiv/early/2020/02/17/2020.02.17.951822.full.pdf

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Concepts: Histone deacetylase, Nucleosome, Cell biology, Acetylation, Biology, Histone, Chemistry, Computational biology, Biochemistry, DNA, Gene

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Cited by: 6

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Citations by year (recent): 2025: 1, 2023: 3, 2021: 2

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References (count): 65

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Related works (count): 10

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