For FY17, we have used multi-dimensional NMR, X-ray crystallography, site-directed mutagenesis coupled with isothermal titration calorimetry to study how nucleosomes and histones are recognized by other proteins. We have determined the cryo-EM structure of the centromere nucleosome core particle bound to the centromere protein CENP-N. We also showed that the reconstituted nucleosome arrays condensed by linker histones or salt have a dynamic structure, which has implications for the structure and function of chromatin in vivo.

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Investigator-Initiated Intramural Research Projects (ZIA)
Project #
1ZIABC010808-11
Application #
9556371
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
11
Fiscal Year
2017
Total Cost
Indirect Cost
Name
Basic Sciences
Department
Type
DUNS #
City
State
Country
Zip Code
Zhou, Bing-Rui; Jiang, Jiansheng; Ghirlando, Rodolfo et al. (2018) Revisit of Reconstituted 30-nm Nucleosome Arrays Reveals an Ensemble of Dynamic Structures. J Mol Biol 430:3093-3110
Chittori, Sagar; Hong, Jingjun; Saunders, Hayden et al. (2018) Structural mechanisms of centromeric nucleosome recognition by the kinetochore protein CENP-N. Science 359:339-343
Fyodorov, Dmitry V; Zhou, Bing-Rui; Skoultchi, Arthur I et al. (2018) Emerging roles of linker histones in regulating chromatin structure and function. Nat Rev Mol Cell Biol 19:192-206
Liu, Chuanbo; Wang, Tianshu; Bai, Yawen et al. (2017) Electrostatic forces govern the binding mechanism of intrinsically disordered histone chaperones. PLoS One 12:e0178405
Zhou, Bing-Rui; Feng, Hanqiao; Ghirlando, Rodolfo et al. (2016) A Small Number of Residues Can Determine if Linker Histones Are Bound On or Off Dyad in the Chromatosome. J Mol Biol 428:3948-3959
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
Zhou, Bing-Rui; Feng, Hanqiao; Ghirlando, Rodolfo et al. (2012) Histone H4 K16Q mutation, an acetylation mimic, causes structural disorder of its N-terminal basic patch in the nucleosome. J Mol Biol 421:30-7

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