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Insight into the architecture of the NuRD complex: structure of the Rbap48-Mta1 subcomplex

DOI: 10.1074/jbc.M114.558940 DOI Help
PMID: 24920672 PMID Help

Authors: Saad S. M. Alqarni (University of Sydney) , Andal Murthy (University of Cambridge) , Wei Zhang (University of Cambridge) , Marcin R. Przewloka (University of Cambridge) , Ana P. G. Silva (University of Sydney) , Aleksandra A. Watson (University of Cambridge) , Sara Lejon Dodd (University of Cambridge) , Xue-Yuan Pei (University of Cambridge) , Arne H. Smits (Department of Molecular Cancer Research, UMC Utrecht) , Susan L. Kloet (UMC Utrecht) , Hongxing Wang (Children's Hospital of Philadelphia) , Nicholas E. Shepherd (University of Sydney) , Philippa H. Stokes (University of Sydney) , Gerd A. Blobel (Children's Hospital of Philadelphia) , Michiel Vermeulen (UMC Utrecht) , David M. Glover (University of Cambridge) , Joel P. Mackay (University of Sydney) , Ernest D. Laue (University of Cambridge)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Biological Chemistry , VOL 289 (32) , PAGES 21844 - 21855

State: Published (Approved)
Published: August 2014
Diamond Proposal Number(s): 9537

Open Access Open Access

Abstract: The nucleosome remodeling and deacetylase (NuRD) complex is a widely conserved transcriptional co-regulator that harbors both nucleosome remodeling and histone deacetylase activities. It plays a critical role in the early stages of ES cell differentiation and the reprogramming of somatic to induced pluripotent stem cells. Abnormalities in several NuRD proteins are associated with cancer and aging. We have investigated the architecture of NuRD by determining the structure of a subcomplex comprising RbAp48 and MTA1. Surprisingly, RbAp48 recognizes MTA1 using the same site that it uses to bind histone H4, showing that assembly into NuRD modulates RbAp46/48 interactions with histones. Taken together with other results, our data show that the MTA proteins act as scaffolds for NuRD complex assembly. We further show that the RbAp48-MTA1 interaction is essential for the in vivo integration of RbAp46/48 into the NuRD complex.

Journal Keywords: Chromatin; Chromatin Structure; Gene Regulation; Protein Assembly; Protein Structure; MTA1; NuRD Complex; RBBP4; RbAp48

Subject Areas: Biology and Bio-materials

Instruments: I04-Macromolecular Crystallography

Added On: 25/02/2015 09:04


Discipline Tags:

Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)