表观遗传调控影响DNA复制、基因转录、DNA损伤修复、基因组稳定性维持等重要生物学事件，并与癌症、自体免疫等疾病密切相关。染色质由DNA和组蛋白组成，染色质结构的动态变化决定DNA的开放和关闭状态，构成表观遗传调控的分子基础。染色质结构的异常导致表观遗传调控错误并导致疾病。研究染色质结构变化规律对于揭示表观遗传机制以及相关的疾病研究具有重要的理论意义和临床应用价值。

　　组蛋白是染色质的重要组成原件，是表观遗传调控的重要参与者。组蛋白在基因组上的装配、移除、交换等变化会造成染色质结构的变化，组蛋白在细胞内的修饰、转运、存贮等过程受到组蛋白伴侣、组蛋白修饰酶、染色质重塑复合物等表观因子的调控。本课题组主要研究组蛋白在染色质结构变化与表观遗传调控中的功能，主要方向包括：（1）染色质组装（2）染色质结构维持（3）组蛋白变体和修饰的识别。本课题组利用多种结构生物学手段，并结合生物化学、生物物理学、酵母遗传学等方法进行研究。

  主页：http://www.ibp.cas.cn/ktzz/ktzz_Z/201308/t20130829_3920653.html, Email:zhouzh@ibp.ac.cn, Tel:010-64889862，

欢迎对表观遗传和结构生物学研究感兴趣的同学加入我们的集体！

071010-生物化学与分子生物学
071007-遗传学
071011-生物物理学

染色质结构及表观调控
结构生物学
蛋白质工程

1999-09--2003-08   中科院上海生物化学与细胞生物学研究所   理学博士
1992-09--1999-07   湖南师范大学   理学学士硕士

   

2008-09~2011-09,美国国立健康研究院癌症研究所, Research Fellow
2003-09~2008-09,美国国立健康研究院癌症研究所, Visiting Fellow

2018-08-01-2021-10-31,中国生物物理学会11届理事会, 会员工作委员会主任
2017-11-30-今,《生命科学研究》学术期刊, 编委

结构生物学技术
细胞的物理生物学
高等生物物理学

   

   

[1] 周政. 周政：因材施教 因地制宜 寓研于乐. 中国科技教育[J]. 2022, 34-35, http://lib.cqvip.com/Qikan/Article/Detail?id=7106845778.
[2] Shi, Liuxin, Huang, Li, Long, Haizhen, Song, Aoqun, Zhou, Zheng. Structural basis of nucleosomal H4K20 methylation by methyltransferase SET8. FASEB JOURNAL[J]. 2022, 36(6): http://dx.doi.org/10.1096/fj.202101821R.
[3] Jiao Chen, Zheng. Epstein-Barr virus protein BKRF4 restricts nucleosome assembly to suppress host antiviral responses. Proceedings of the National Academy of Sciences of the United States of America[J]. 2022, [4] Dai, Linchang, Xiao, Xue, Pan, Lu, Shi, Liuxin, Xu, Ning, Zhang, Zhuqiang, Feng, Xiaoli, Ma, Lu, Dou, Shuoxing, Wang, Pengye, Zhu, Bing, Li, Wei, Zhou, Zheng. Recognition of the inherently unstable H2A nucleosome by Swc2 is a major determinant for unidirectional H2A.Z exchange. CELL REPORTS[J]. 2021, 35(8): http://dx.doi.org/10.1016/j.celrep.2021.109183.
[5] Zhou, Ning, Shi, Liuxin, Shan, Shan, Zhou, Zheng. Molecular basis for the selective recognition and ubiquitination of centromeric histone H3 by yeast E3 ligase Psh1. JOURNAL OF GENETICS AND GENOMICS[J]. 2021, 48(6): 463-472, http://dx.doi.org/10.1016/j.jgg.2021.04.007.
[6] Zhou, Min, Dai, Linchang, Li, Chengmin, Shi, Liuxin, Huang, Yan, Guo, Zhenqian, Wu, Fei, Zhu, Ping, Zhou, Zheng. Structural basis of nucleosome dynamics modulation by histone variants H2A.B and H2AZ2.2. EMBO JOURNAL[J]. 2021, 40(1): http://dx.doi.org/10.15252/embj.2020105907.
[7] Dai, Linchang, Dai, Yaxin, Han, Jinhua, Huang, Yan, Wang, Longge, Huang, Jun, Zhou, Zheng. Structural insight into BRCA1-BARD1 complex recruitment to damaged chromatin. MOLECULAR CELL[J]. 2021, 81(13): 2765-+, http://dx.doi.org/10.1016/j.molcel.2021.05.010.
[8] Huang, Yan, Sun, Lu, Pierrakeas, Leonidas, Dai, Linchang, Pan, Lu, Luk, Ed, Zhou, Zheng. Role of a DEF/Y motif in histone H2A-H2B recognition and nucleosome editing. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA[J]. 2020, 117(7): 3543-3550, https://www.webofscience.com/wos/woscc/full-record/WOS:000514096400035.
[9] Huang, Yan, Dai, Yaxin, Zhou, Zheng. Mechanistic and structural insights into histone H2A-H2B chaperone in chromatin regulation. BIOCHEMICAL JOURNALnull. 2020, 477(17): 3367-3386, https://www.webofscience.com/wos/woscc/full-record/WOS:000582386500016.
[10] Dai, Yaxin, Zhang, Fan, Wang, Longge, Shan, Shan, Gong, Zihua, Zhou, Zheng. Structural basis for shieldin complex subunit 3?mediated recruitment of the checkpoint protein REV7 during DNA double-strand break repair. JOURNAL OF BIOLOGICAL CHEMISTRY[J]. 2020, 295(1): 250-262, https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6952594/.
[11] Gao, Ying, Ren, RuJing, Zhong, ZiLin, Dammer, Eric, Zhao, QianHua, Shan, Shan, Zhou, Zheng, Li, Xia, Zhang, YueQi, Cui, HaiLun, Hu, YongBo, Chen, ShengDi, Chen, JianJun, Guo, QiHao, Wang, Gang. Mutation profile of APP, PSEN1, and PSEN2 in Chinese familial Alzheimer's disease. NEUROBIOLOGY OF AGING[J]. 2019, 77: 154-157, http://dx.doi.org/10.1016/j.neurobiolaging.2019.01.018.
[12] Yunyun Wang, Sheng Liu, Lu Sun, Ning Xu, Shan Shan, Fei Wu, Xiaoping Liang, Yingzi Huang, Ed Luk, Carl Wu, Zheng Zhou. Structural insights into histone chaperone Chz1-mediated H2A.Z recognition and histone replacement.. PLoS Biology[J]. 2019, 17(5): http://dx.doi.org/10.1371/journal.pbio.3000277.
[13] Yaxin Dai, Fan Zhang, Longge Wang, Shan Shan, Zihua Gong, Zheng Zhou. Structural basis for shieldin complex subunit 3–mediated recruitment of the checkpoint protein REV7 during DNA double-strand break repair. The Journal of Biological Chemistry. 2019, 295(1): 250-262, http://dx.doi.org/10.1074/jbc.RA119.011464.
[14] Dai, Linchang, Xu, Ning, Zhou, Zheng. NMR investigations on H2A-H2B heterodimer dynamics conferred by histone variant H2A.Z. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS[J]. 2019, 518(4): 752-758, http://dx.doi.org/10.1016/j.bbrc.2019.08.127.
[15] Sun, Wan, Shen, Yanjie, Shan, Shan, Han, Liyun, Li, Yang, Zhou, Zheng, Zhong, Zilin, Chen, Jianjun. Identification of TYR mutations in patients with oculocutaneous albinism. MOLECULAR MEDICINE REPORTS[J]. 2018, 17(6): 8409-8413, https://www.webofscience.com/wos/woscc/full-record/WOS:000435394000118.
[16] Huang Yan, Zhou Zheng. Recent Progress in Histone Chaperones Associated With H2A-H2B Type Histones. PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS[J]. 2018, 45(9): 971-980, https://www.webofscience.com/wos/woscc/full-record/WOS:000445847600010.
[17] Dai, Linchang, Xie, Xiaoyan, Zhou, Zheng. Crystal structure of the histone heterodimer containing histone variant H2A.Bbd. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS[J]. 2018, 503(3): 1786-1791, http://dx.doi.org/10.1016/j.bbrc.2018.07.114.
[18] Yaxin Dai, Aili Zhang, Shan Shan, Zihua Gong, Zheng Zhou. Structural basis for recognition of 53BP1 tandem Tudor domain by TIRR. NATURE COMMUNICATIONS[J]. 2018, 9(1): https://doaj.org/article/a2d88984045941a58372fc19fffd5812.
[19] Huang Yan, Zhou Zheng. Recent Progress in Histone Chaperones Associated With H2A-H2B Type Histones. PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS[J]. 2018, 45(9): 971-980, https://www.webofscience.com/wos/woscc/full-record/WOS:000445847600010.
[20] Liang, Xiaoping, Shan, Shan, Pan, Lu, Zhao, Jicheng, Ranjan, Anand, Wang, Feng, Zhang, Zhuqiang, Huang, Yingzi, Feng, Hanqiao, Wei, Debbie, Huang, Li, Liu, Xuehui, Zhong, Qiang, Lou, Jizhong, Li, Guohong, Wu, Carl, Zhou, Zheng. Structural basis of H2A.Z recognition by SRCAP chromatin-remodeling subunit YL1. NATURE STRUCTURAL & MOLECULAR BIOLOGY[J]. 2016, 23(4): 317-323, http://dx.doi.org/10.1038/nsmb.3190.
[21] Zhong, Zilin, Yan, Min, Sun, Wan, Wu, Zehua, Han, Liyun, Zhou, Zheng, Zheng, Fang, Chen, Jianjun. Two novel mutations in PRPF3 causing autosomal dominant retinitis pigmentosa. SCIENTIFIC REPORTS[J]. 2016, 6: http://dx.doi.org/10.1038/srep37840.
[22] Zhou JuJun, Feng XiaoLi, Zhou Zheng. Chromatin Assembly of Histone Variants. PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS[J]. 2015, 42(11): 1003-1008, https://www.webofscience.com/wos/woscc/full-record/WOS:000365558600004.
[23] Mao, Zhuo, Pan, Lu, Wang, Weixiang, Sun, Jian, Shan, Shan, Dong, Qiang, Liang, Xiaoping, Dai, Linchang, Ding, Xiaojun, Chen, She, Zhang, Zhuqiang, Zhu, Bing, Zhou, Zheng. Anp32e, a higher eukaryotic histone chaperone directs preferential recognition for H2A.Z. CELL RESEARCH[J]. 2014, 24(4): 389-399, http://dx.doi.org/10.1038/cr.2014.30.
[24] Hong, Jingjun, Feng, Hanqiao, Zhou, Zheng, Ghirlando, Rodolfo, Bai, Yawen. Identification of Functionally Conserved Regions in the Structure of the Chaperone/CenH3/H4 Complex. JOURNAL OF MOLECULAR BIOLOGY[J]. 2013, 425(3): 536-545, http://dx.doi.org/10.1016/j.jmb.2012.11.021.
[25] Zhou, Zheng, Feng, Hanqiao, Zhou, BingRui, Ghirlando, Rodolfo, Hu, Kaifeng, Zwolak, Adam, Jenkins, Lisa M Miller, Xiao, Hua, Tjandra, Nico, Wu, Carl, Bai, Yawen. Structural basis for recognition of centromere histone variant CenH3 by the chaperone Scm3. NATURE[J]. 2011, 472(7342): 234-237, https://www.webofscience.com/wos/woscc/full-record/WOS:000289469100046.
[26] Hansen, D Flemming, Zhou, Zheng, Fen, Haniqiao, Jenkins, Lisa M Miller, Bai, Yawen, Kay, Lewis E. Binding Kinetics of Histone Chaperone Chz1 and Variant Histone H2A.Z-H2B by Relaxation Dispersion NMR Spectroscopy. JOURNAL OF MOLECULAR BIOLOGY[J]. 2009, 387(1): 1-9, http://dx.doi.org/10.1016/j.jmb.2009.01.009.
[27] Zhou, Zheng, Feng, Hanqiao, Ghirlando, Rodolfo, Bai, Yawen. The High-Resolution NMR Structure of the Early Folding Intermediate of the Thermus thermophilus Ribonuclease H. JOURNAL OF MOLECULAR BIOLOGY[J]. 2008, 384(2): 531-539, http://dx.doi.org/10.1016/j.jmb.2008.09.044.
[28] Zhou, Zheng, Feng, Hanqiao, Hansen, D Flemming, Kato, Hidenori, Luk, Ed, Freedberg, Daron I, Kay, Lewis E, Wu, Carl, Bai, Yawen. NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B. NATURE STRUCTURAL & MOLECULAR BIOLOGY[J]. 2008, 15(8): 868-869, https://www.webofscience.com/wos/woscc/full-record/WOS:000258191100023.
[29] Zheng Zhou, Hanqiao Feng, Yawen Bai. Detection of a hidden folding intermediate in the focal adhesion target domain: Implications for its function and folding. Proteins. 2006, [30] Feng, HQ, Zhou, Z, Bai, YW. A protein folding pathway with multiple folding intermediates at atomic resolution. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA[J]. 2005, 102(14): 5026-5031, https://www.webofscience.com/wos/woscc/full-record/WOS:000228195800021.
[31] Zheng Zhou. Structure determination and folding pathway characterization of an engineered multi-domain protein: kinetic versus equilibrium intermediates. Biochemistry-US. 2005, [32] Zheng Zhou. The folding pathway of Rd-apocyt b562: Demonstration of the on-pathway nature of a hidden intermediate and characterization of the rate-limiting transition state by protein. J. Mol. Biol.. 2005, 

（1） 蛋白质折叠方法学：利用氢氘交换介导的蛋白质工程富集蛋白折叠中间体及利用核磁共振进行结构研究, Protein folding protocols: Population and structure determination of hidden folding intermediates by native-state hydrogen exchange-directed protein engineering and nuclear magnetic resonance, Humana Press, 2006-02, 第 3 作者

   

（ 1 ） 组蛋白变体结构及其参与的表观遗传调控机理研究, 主持, 国家级, 2012-01--2015-12
（ 2 ） 组蛋白二聚体的动态结构及其生物学功能研究, 主持, 国家级, 2013-01--2016-12
（ 3 ） 表观遗传信息建立与解读的分子基础, 参与, 国家级, 2015-01--2016-08
（ 4 ） 染色质结构及其调控, 参与, 国家级, 2016-01--2021-12
（ 5 ） 染色质重构复合物SRCAP/SWR1介导的H2A.Z染色质组装机制研究, 主持, 国家级, 2017-01--2020-12

（1）Preferential recognition of H2A.Z-H2B by Mps3 direct DNA double-strand breaks to nuclear periphery   2017-09-06
（2）Structural basis of H2A.Z recognition by SRCAP subunit YL1   2016-07-28
（3）Structural basis of H2A.Z recognition by SRCAP chromatin-remodeling subunit YL1   Zheng Zhou   2016-05-09
（4）Structural basis of H2A.Z recognition by its chaperones   2016-04-09
（5）Structural study of H2A.Z specific histone chaperone   2014-08-04
（6）Structural basis for recognition of centromere specific histone H3 variant by nonhistone Scm3   Zheng Zhou, Hanqiao Feng, Yawen Bai   2010-03-01

已指导学生

梁小平  博士研究生  071010-生物化学与分子生物学  

潘露  博士研究生  071010-生物化学与分子生物学  

王云云  博士研究生  071010-生物化学与分子生物学  

谢晓燕  博士研究生  071010-生物化学与分子生物学  

周驹俊  博士研究生  071010-生物化学与分子生物学  

吴飞  硕士研究生  085238-生物工程  

戴亚鑫  博士研究生  071010-生物化学与分子生物学  

黄艳  博士研究生  071010-生物化学与分子生物学  

现指导学生

黄莉  博士研究生  071010-生物化学与分子生物学  

周宁  博士研究生  071010-生物化学与分子生物学  

谌姣  博士研究生  071010-生物化学与分子生物学  

周英博  硕士研究生  077802-免疫学  

史刘歆  博士研究生  071010-生物化学与分子生物学  

王龙歌  博士研究生  071010-生物化学与分子生物学  

朱浩强  博士研究生  071010-生物化学与分子生物学