Poster Presentation The 42nd Lorne Conference on Protein Structure and Function 2017

Architecture of the Nucleosome Remodeling and Deacetylase (NuRD) complex (#290)

Ana PG Silva 1 , Jason KK Low 1 , Mario Torrado 1 , Sarah R Webb 1 , Mehdi S Tabar 1 , Jason Schmidberger 1 , Lou Brillault 2 , Nicholas E Shepherd 2 , Michael J Landsberg 2 , Joel P Mackay 1
  1. University of Sydney, NSW, Australia
  2. Institute for Molecular Biosciences, University of Queensland, Brisbane, Queensland, Australia

The nucleosome remodeling and deacetylase (NuRD) complex regulates both gene transcription and DNA damage repair. It is essential for normal development and is found in all complex animals. The NuRD complex is composed of six proteins, for which different paralogues can be present. The complex contains a total of 10-11 subunits with a total molecular weight of around 1 MDa. These subunits include the remodeler Chromatin Helicase DNA-binding protein 4 (CHD4, or CHD3/5), the histone deacetylases HDAC1 and HDAC2, the WD40-repeat protein RBBP4 and RBBP7, the metastasis associated proteins MTA1 (MTA2 and/or MTA3), the poorly characterized proteins GATAD2A or GATAD2B, and the methyl-DNA binding domain proteins MBD2 or MBD3. However, it is still not well defined how the complex is assembled or how the subunits combine to act on their chromatin substrate. Here, we present structural approaches to determine the 3D architecture of the NuRD complex.