2001– 2006 Ph.D. Biochemistry and Molecular Biology, School of Life Sciences, Peking University, Beijing, China
1997– 2001 B.S. Biochemistry and Molecular Biology, School of Life Sciences, Peking University, Beijing, China
2019.02 - Present Tenured Professor,School of Life Sciences, Peking University, Beijing, China
2018.02 - 2019.02 Tenured Associate Professor,School of Life Sciences, Peking University, Beijing, China
2012.01 - 2018.01 Assistant Professor, School of Life Sciences, Peking University, Beijing, China
2012.01 - Present Investigator, Peking-Tsinghua Center For Life Sciences, Peking University, Beijing, China
2011.04 –2011.12 Research Associate, Mayo Clinic College of Medicine, Rochester, MN, USA
2009.01 –2011.03 Senior research Fellow, Mayo Clinic College of Medicine, Rochester, MN, USA
2006.09 –2008.12 Research Fellow, Mayo Clinic College of Medicine, Rochester, MN, USA
Honors and Awards
2017 National Science Fund for Distinguished Young Scholars
2014 Bayer Investigator Award
2013 National Science Fund for Outstanding Young Scholars
2009 Kendall-Mayo Fellowship
How epigenetic states defined by chromatin organization are inherited remains one of the most enigmatic, yet fundamental questions in the field of chromatin research. Accumulated data show that dysregulation of this process is linked to various diseases, including cancer and premature aging. The long-term goals of my laboratory’s research are aimed at addressing:
1) how epigenetic information, defined by chromatin structures, is inherited during mitotic cell division;
2) how this process is involved in maintaining genome integrity;
3) how this process goes awry in human disease.
Specifically, using both yeast and mammalian cells, we will determine how nucleosomes, the basic repeating units of chromatin, are disassembled/reassembled in a process coupled to DNA replication and how DNA replication-coupled (RC) nucleosome dynamics impacts epigenetic silencing. These studies will utilize combinatorial tools including genetics and genomics approaches to dissect the detailed mechanisms driving this crucial process. Answers to these questions will not only have significant scientific value, but will also likely lead to the discovery of novel drug targets for the treatment of cancer caused by epigenetic alterations.
Representative Peer-Reviewed Publications
1. Li, S.Q#., Dong, Z.Q#., Yang, S.S., Feng, J.X., and Li, Q*. (2019) Chaperoning RPA during DNA metabolism. Current Genetics doi: 10.1007/s00294-019-00945-3
2. Li, Q*., Zhang, X., and Zhang, Z.* (2018). CHAF1B overexpression: A brake for the differentiation of leukemia cells. Cancer Cell 34:693-694.
3. Li, S.Q#, Xu, Z.Y. #, Xu, J.W. #, Zuo, L.Y., Yu, C.H., Zheng, P., Gan, H.Y., Wang, X.Z., Li, L.T., Sharma, S., Chabes, A., Li, D., Wang, S., Zheng, S.H., Li, J.B., Chen, X.F., Sun, Y.J., Xu, D.Y., Han, J.H., Chan, K.M., Qi, Z., Feng, J.X.*, and Li, Q.* (2018) Rtt105 functions as a chaperone for replication protein A to preserve genome stability The EMBO Journal e99154.
4. Yan, X.W#., Yang, J.Y#., Xu, J.W#., Feng, J.X*., and Li, Q.* (2018). Histone chaperone Spt16p is required for heterochromatin mediated silencing in budding yeast. Protein & Cell 9:652-658.
5. Gao, S.X., Feng, S.M., Ning, S.K., Liu, J.Y., Zhao, H.Y., Xu, Y.X., Shang, J.F., Li, K.J., Li, Q., Guo, R., & Xu, D.Y. (2018) An OB-fold complex controls the repair pathways for DNA double-strand breaks. Nature Communications 9: 3925.
6. Liu, S.F.#, Xu, Z.Y. #, Leng, H. #, Zheng, P., Yang, J.Y., Chen, K.F., Feng, J.X., Li, Q. * (2017). RPA binds histone H3-H4 and functions in DNA replication-coupled nucleosome assembly. Science 355, 415-420.
7. Li, W.＃, Chen, P.＃, Yu, J., Dong, L.P., Liang, D., Feng, J.X., Yan, J., Wang, P.Y., Li, Q., Zhang, Z.G., Li, M.*, and Li, G.H.* (2016). FACT remodels the tetranucleosomal unit of chromatin fibers for gene transcription. Molecular Cell 64, 120-133.
8. Feng, J.X.＃, Gan, H.Y.＃, Eaton, M.L., Zhou, H., Li, S.Q., Belsky, J.A., MacAlpine, D.M., Zhang, Z.G.* and Li, Q.* (2016). Noncoding transcription is a driving force for nucleosome instability in spt16 mutant cells. Molecular and Cellular Biology 36, 1856-1867. Article of significant interest selected as a Spotlight.
9. Yang, J.Y.＃, Zhang, X.＃, Feng, J.X.＃, Leng, H., Li, S.Q., Xiao, J.X., Liu, S.F., Xu, Z.Y., Xu, J.W., Li, D., Wang, Z.S., Wang, J.Y., and Li, Q.* (2016). The Histone Chaperone FACT Contributes to DNA Replication-Coupled Nucleosome Assembly. Cell Reports 14, 1128-1141.
10. Zhang, X., and Li, Q.* (2014). A role of histone modifications during chromatin replication. Chinese Bulletin of Life Sciences 26, 1176-1186. (In Chinese)
11. Su, D.#, Hu, Q.#, Li, Q.#, Thompson, J.R., Cui, G.F., Fazly, A., Davies, B.A., Botuyan, M.V., Zhang, Z.G.* and Mer, G.* (2012). Structural basis for recognition of H3K56-acetylated histone H3–H4 by the chaperone Rtt106. Nature 483, 104-107 (# Co-first author).
12. Li, Q.＃, Burgess, R.＃, and Zhang, Z.G.* (2012). All roads lead to chromatin: Multiple pathways for histone deposition. Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms. 1819, 238-46 (# Co-first author).
13. Li, Q., and Zhang, Z.G.* (2012). Linking DNA replication to heterochromatin silencing and epigenetic inheritance. Acta Biochimica et Biophysica Sinica (ABBS) 44, 3-13. This review was selected as the cover story.
14. Fazly, A., Li, Q., Hu, Q., Mer, G., Horazdovsky, B. and Zhang, Z.G.* (2012). Histone chaperone Rtt106 promotes nucleosome formation using (H3-H4)2 tetramers. The Journal of Biological Chemistry 2287, 10753-10760.
15. Burgess, R., Zhou, H., Han, J.H., Li, Q., and Zhang, Z.G.* (2012). The SCFDia2 ubiquitin E3 ligase ubiquitylates Sir4 and functions in transcriptional silencing. PLoS Genetics 8, e1002846
16. Han, J.H., Li, Q., McCullough, L., Formosa, T. and Zhang, Z.G.* (2010). Ubiquitylation of FACT by the Cullin-E3 ligase Rtt101 connects FACT to DNA replication. Genes & Development 24, 1485-1490.
17. Li, Q., Fazly, A., Zhou, H., Huang, H.S., Zhang, Z.G.* and Stillman, B.* (2009). The Elongator complex interacts with PCNA and modulates transcriptional silencing and sensitivity to DNA damage agents. PLoS Genetics 5, e1000684.
18. Li, Q.＃, Zhou, H.＃, Wurtele, H., Davies, B., Horazdovasky, B., Verreault, A.* and Zhang, Z.G.* (2008). Acetylation of Histone H3 lysine 56 regulates CAF-1 dependent nucleosome assembly. Cell 134,244-255 (# Co-first author). Previewed in the same issue. Highlighted in Nature Reviews Molecular Cell Biology, September 2008