Abstract

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.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Investigator-Initiated Intramural Research Projects (ZIA)
Project #
1ZIABC010808-06
Application #
8552841
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
6
Fiscal Year
2012
Total Cost
$855,129
Indirect Cost

  Institution

Name
National Cancer Institute Division of Basic Sciences
Department
Type
DUNS #
City
State
Country
Zip Code

  Publications

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

Showing the most recent 10 out of 13 publications