Structural studies of chromatin assembly/disassembly: Our current research is focussed on studies of two key protein complexes involved in chromatin structure; Chromatin Assembly Factor–1 (CAF–1), which assembles histones H3/H4 into DNA in the first step of nucleosome assembly, and the Nucleosome Remodelling Deacetylase complex (NuRD), which shares two subunits RbAp46 and RbAp48 (pRB–associated proteins p46 and p48, also known as RBBP7 and RBBP4, respectively). RbAp46 and RbAp48 are highly homologous histone chaperones, which belong to the WD40–repeat protein family and they are found in a large number of different complexes that either covalently modify histones or aid their assembly into nucleosomes.
- Structural plasticity of histones H3–H4 facilitates their allosteric exchange between RbAp48 and ASF1, Zhang W, Tyl M, Ward R, Sobott F, Maman J, Murthy AS, Watson AA, Fedorov O, Bowman A, Owen-Hughes T, EL-Mkami H, Murzina NV, Norman D, Laue ED, Nat Struct Mol Biol, 2013, 20 (1): 29-35
- The PHD and Chromo Domains Regulate the ATPase Activity of the Human Chromatin Remodeler CHD4, Watson AA, Mahajan P, Mertens HD, Deery MJ, Zhang W, Pham P, Du X, Bartke T, Edlich C, Berridge G, Chen Y, Burgess-Brown NA, Kouzarides T, Wiechens N, Owen-Hughes T, Svergun DI, Gileadi O, Laue ED, J Mol Biol, 2012, 422 (1): 3-17
- Insights into Association of the NuRD Complex with FOG-1 from the Crystal Structure of an RbAp48 FOG-1 Complex, Lejon S, Thong SY, Murphy A, AlQarni S, Murzina NV, Blobel GA, Laue ED, Mackay JD, Journal of Biological Chemistry, 2011, 286(2):1196-203