Structure and function insights into the NuRD chromatin remodeling complex.

Abstract

Transcription regulation through chromatin compaction and decompaction is regulated through various chromatin-remodeling complexes such as nucleosome remodeling and histone deacetylation (NuRD) complex. NuRD is a 1 MDa multi-subunit protein complex which comprises many different subunits, among which histone deacetylases HDAC1/2, ATP-dependent remodeling enzymes CHD3/4, histone chaperones RbAp46/48, CpG-binding proteins MBD2/3, the GATAD2a (p66α) and/or GATAD2b (p66β) and specific DNA-binding proteins MTA1/2/3. Here, we review the currently known crystal and NMR structures of these subunits, the functional data and their relevance for biomedical research considering the implication of NuRD subunits in cancer and various other diseases. The complexity of this macromolecular assembly, and its poorly understood mode of interaction with the nucleosome, the repeating unit of chromatin, illustrate that this complex is a major challenge for structure-function relationship studies which will be tackled best by an integrated biology approach.

• Authors: Morgan P Torchy, Ali Hamiche, Bruno P Klaholz
• Journal: Cellular and molecular life sciences : CMLS (Cell Mol Life Sci) Vol. 72 Issue 13 Pg. 2491-507 (Jul 2015) ISSN: 1420-9071 [Electronic] Switzerland
• PMID: 25796366 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)

Chemical References

• DNA-Binding Proteins
• Histone Chaperones
• Histone Deacetylases
• Mi-2 Nucleosome Remodeling and Deacetylase Complex

Topics

• Chromatin Assembly and Disassembly (genetics, physiology)
• DNA Methylation
• DNA-Binding Proteins (chemistry, metabolism)
• Gene Expression Regulation (physiology)
• Histone Chaperones (chemistry, metabolism)
• Histone Deacetylases (chemistry, metabolism)
• Humans
• Mi-2 Nucleosome Remodeling and Deacetylase Complex (chemistry, genetics, metabolism)
• Models, Molecular
• Protein Conformation