For FY12, we have used multi-dimensional NMR and site-directed mutagenesis methods to assign the chemical shifts of methyl groups of Val, Leu, and Ile of histones in the nucleosome. They were used as probes for studying the dynamics of nucleosome and its interactions with other proteins such as linker histone H1 and high mobility group nucleosomal proteins (HMGN), kinetochore protein CENP-C. We have determined the structure of the HMGN2-nucleosome complex. We have also investigated the structure of Scm3 complexed with centromere histone variant Cse4 and histone H4. Our studies are important for understanding how chromosomes are segregated during cell division.
|Zhou, Bing-Rui; Jiang, Jiansheng; Feng, Hanqiao et al. (2015) Structural Mechanisms of Nucleosome Recognition by Linker Histones. Mol Cell 59:628-38|
|Hong, Jingjun; Feng, Hanqiao; Wang, Feng et al. (2014) The catalytic subunit of the SWR1 remodeler is a histone chaperone for the H2A.Z-H2B dimer. Mol Cell 53:498-505|
|Hong, Jingjun; Feng, Hanqiao; Zhou, Zheng et al. (2013) Identification of functionally conserved regions in the structure of the chaperone/CenH3/H4 complex. J Mol Biol 425:536-45|
|Kato, Hidenori; Jiang, Jiansheng; Zhou, Bing-Rui et al. (2013) A conserved mechanism for centromeric nucleosome recognition by centromere protein CENP-C. Science 340:1110-3|
|Chu, Xiakun; Wang, Yong; Gan, Linfeng et al. (2012) Importance of electrostatic interactions in the association of intrinsically disordered histone chaperone Chz1 and histone H2A.Z-H2B. PLoS Comput Biol 8:e1002608|
|Kato, Hidenori; van Ingen, Hugo; Zhou, Bing-Rui et al. (2011) Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR. Proc Natl Acad Sci U S A 108:12283-8|
|Zhou, Zheng; Feng, Hanqiao; Zhou, Bing-Rui et al. (2011) Structural basis for recognition of centromere histone variant CenH3 by the chaperone Scm3. Nature 472:234-7|