Current position:

LEI Ming

Executive Director, Professor, Principal Investigator

Research direction:Common mechanism driving spermatogenesis, early embryo development and tumorigenesis in primates

Research Interests
Research Interests and Honors
The goal of Prof. Lei’s laboratory is to understand the organization and dynamics of macromolecular assemblies important for genome regulation and stability. With combination of structural analyses, such as X-ray crystallography, nuclear magnetic resonance and electron microscopy, coupled with biophysical and biochemical experimentation, his laboratory has made important progress on telomeres and epigenetics. He had published more than 70 SCI papers and had the experience of leading the Ministry of Science and Technology 973 Program of China and the National Natural Science Foundation Key Program and Joint Funds of Key Program of China, and participating in the Strategic Priority Research Program of the Chinese Academy of Sciences and the National Science and Technology Major Project ‘Key New Drug Creation and Manufacturing Program’ of China. In 2009, he got the Howard Hughes Medical Institute Early Career Award. In 2011, he was honored the Recruitment Program of Global Experts by the Organization Department of the CPC Central Committee, China. In 2015, he was supported by National Natural Science Foundation for Distinguished Young Scholars of China.
Education and Work Experience
1996/09 – 2001/05, Harvard University, School of Medicine
Ph.D., Biophysics
1994/09 – 1996/05, McGill University, Department of Physics
M.Sc., Physics
1989/09 – 1994/07, Tsinghua University, Department of Modern Applied Physics
B.S., Modern Applied Physics, Electronics and Computer Technology

Work Experience
2017/09 – Present, Shanghai Institute of Precision Medicine, Ninth People’s Hospital, Shanghai Jiao Tong University School of Medicine
2011/06 – 2017/09, Shanghai Institute of Biochemistry and Cell Biology, SIBS, CAS
2010/09 – 2011/06, University of Michigan, Department of Biochemistry
Associate Professor (tenured)
2009/01 – 2011/06, Howard Hughes Medical Institute (HHMI)
Early Career Scientist
2004/11 – 2010/09, University of Michigan, Department of Biochemistry
Assistant Professor (tenure track)
2001/11 – 2004/11, University of Colorado, Department of Chemistry and Biochemistry

2017/09 – Present, Shanghai Institute of Precision Medicine, Ninth People’s Hospital, Shanghai Jiao Tong University School of Medicine
Executive Director
2011/06 – 2017/09, Shanghai Institute of Biochemistry and Cell Biology, SIBS, CAS
Deputy Director
2011/06 – 2017/09, National Center for Protein Science Shanghai, SIBCB, SIBS, CAS

Selected Publications

Chen H#, Xue J#, Churikov D, Hass EP, Shi S, Lemon LD, Luciano P, Bertuch AA, Zappulla DC, Geli V, Wu J*, and Lei M* Structural insights into yeast telomerase recruitment to telomeres. Cell. 2018, 172(1-2), 331-343 e13.

Xue J#, Chen H#, Wu J, Takeuchi M, Inoue H, Liu Y, Sun H, Chen Y*, Kanoh J*, and Lei M* Structure of the fission yeast S. pombe telomeric Tpz1-Poz1-Rap1 complex. Cell Res. 2017, 27(12), 1503-20.

Hu C#, Rai R#, Huang C, Broton C, Long J, Xu Y, Xue J, Lei M*, Chang S*, and Chen Y* Structural and functional analyses of the mammalian TIN2-TPP1-TRF2 telomeric complex. Cell Res. 2017, 27(12), 1485-502.

Long J#, Huang C#, Chen Y, Zhang Y, Shi S, Wu L, Liu Y, Liu C, Wu J*, and Lei M* Telomeric TERB1-TRF1 interaction is crucial for male meiosis. Nat Struct Mol Biol. 2017, 24(12), 1073-80.

Chen C#, Gu P#, Wu J, Chen X, Niu S, Sun H, Wu L, Li N, Peng J, Shi S, Fan C, Huang M, Wong CCL, Gong Q, Kumar-Sinha C, Zhang R, Pusztai L, Rai R, Chang S*, and Lei M* Structural insights into POT1-TPP1 interaction and POT1 C-terminal mutations in human cancer. Nat Commun. 2017, 8:14929.

Rai R#, Hu C, Broton C, Chen Y, Lei M*, and Chang S* NBS1 phosphorylation status dictates repair choice of dysfunctional telomeres. Mol Cell. 2017, 65(5): 801-17.

Yin J#, Wan B#, Sarkar J#, Horvath K, Wu J, Chen Y, Cheng G, Wan K, Chin P, Lei M*, and Liu Y* Dimerization of SLX4 contributes to functioning of the SLX4-nuclease complex. Nucleic Acids Res. 2016, 44(10): 4871-80.

Li Y#, Han J, Zhang Y, Cao F, Liu Z, Li S, Wu J, Hu C, Wang Y, Shuai J, Chen J, Cao L, Li D, Shi P, Tian C, Zhang J, Dou Y, Li G*, Chen Y*, and Lei M* Structural basis for activity regulation of MLL family methyltransferases. Nature. 2016, 530(7591): 447-52.

Wan B#, Tang T#, Upton H, Shuai J, Zhou Y, Li S, Chen J, Brunzelle JS, Zeng Z, Collins K, Wu J*, and Lei M* The Tetrahymena telomerase p75-p45-p19 subcomplex is a unique CST complex. Nat Struct Mol Biol. 2015, 22(12): 1023-6.

Sarkar J#, Wan B, Yin J, Vallabhaneni H, Horvath K, Kulikowicz T, Bohr VA, Zhang Y, Lei M*, and Liu Y* SLX4 contributes to telomere preservation and regulated processing of telomeric joint molecule intermediates. Nucleic Acids Res. 2015, 43(12): 5912-23.

Deng W#, Wu J#, Wang F#, Kanoh J, Dehe PM, Inoue H, Chen J, and Lei M* Fission yeast telomere-binding protein Taz1 is a functional but not a structural counterpart of human TRF1 and TRF2. Cell Res. 2015, 25(7): 881-4.

Huang J#, Brown A, Wu J, Xue J, Bley C, Rand D, Wu L, Zhang R, Chen J*, and Lei M* Structural Basis for Protein-RNA Recognition in Telomerase. Nat Struct Mol Biol. 2014, 21(6): 507-12.

Wan B#, Yin J#, Horvath K#, Sarkar J, Chen Y, Wu J, Wan K, Lu J, Gu P, Yu EY, Lue NF, Chang S, Liu Y*, and Lei M* SLX4 assembles a telomere maintenance toolkit by bridging multiple endonucleases with telomeres. Cell Rep. 2013, 4(5): 861-9.

Yu EY#, Sun J#, Lei M*, and Lue NF* Analyses of Candida Cdc13 orthologues revealed a novel OB fold dimer arrangement dimerization-assisted DNA binding and substantial structural differences between Cdc13 and RPA70. Mol Cell Biol. 2012, 32(1): 186-98.

Huang J#, Wan B, Wu L, Yang Y, Dou Y, and Lei M* Structural insight into the regulation of MOF in the male-specific lethal complex and the non-specific lethal complex. Cell Res. 2012, 22(6): 1078-81.

Huang J#, Gurung B, Wan B, Matkar S, Veniaminova NA, Wan K, Merchant JL, Hua X*, and Lei M* The same pocket in menin binds both MLL and JUND but has opposite effects on transcription. Nature. 2012, 482(7386): 542-6.

Chen Y#, Cao F, Wan B, Dou Y, and Lei M* Structure of the SPRY domain of human Ash2L and its interactions with RbBP5 and DPY30. Cell Res. 2012, 22(3): 598-602.

Zeng Z#, Min B#, Huang J, Hong K, Yang Y, Collins K*, and Lei M* Structural basis for Tetrahymena telomerase processivity factor Teb1 binding to single-stranded telomeric-repeat DNA. Proc Natl Acad Sci U S A. 2011, 108(51): 20357-61.

Sun J#, Yang Y, Wan K, Mao N, Yu TY, Lin YC, DeZwaan DC, Freeman BC, Lin JJ, Lue NF, and Lei M* Structural bases of dimerization of yeast telomere protein Cdc13 and its interaction with the catalytic subunit of DNA polymerase alpha. Cell Res. 2011, 21(2): 258-74.

Chen Y#, Wan B#, Wang KC#, Cao F, Yang Y, Protacio A, Dou Y, Chang HY, and Lei M* Crystal structure of the N-terminal region of human Ash2L shows a winged-helix motif involved in DNA binding. EMBO Rep. 2011, 12(8): 797-803.

Chen Y#, Rai R#, Zhou ZR, Kanoh J, Ribeyre C, Yang Y, Zheng H, Damay P, Wang F, Tsujii H, Hiraoko Y, Shore D, Hu H, Chang S*, and Lei M* A conserved motif within RAP1 has diversified roles in telomere protection and regulation in different organisms. Nat Struct Mol Biol. 2011, 18(2): 213-21.

Zeng Z#, Wang W#, Yang Y, Chen Y, Yang X, Diehl JA, Liu X*, and Lei M* Structural basis of selective ubiquitination of TRF1 by SCFFbx4. Dev Cell. 2010, 18(2): 214-25.

Wang F#, Yang Y, Singh TR, Busygina V, Guo R, Wan K, Wang W, Sung P, Meetei AR, and Lei M* Crystal structures of RMI1 and RMI2 two OB-fold regulatory subunits of the BLM complex. Structure. 2010, 18(9): 1159-70.

Cao F#, Chen Y#, Cierpicki T, Liu Y, Basrur V, Lei M*, and Dou Y* An Ash2L/RbBP5 heterodimer stimulates the MLL1 methyltransferase activity through coordinated substrate interactions with the MLL1 SET domain. PLoS One. 2010, 5(11): e14102.

Wang W#, Yang Y, Gao Y, Xu Q, Wang F, Zhu S, Old W, Resing K, Ahn N, Lei M*, and Liu X* Structural and mechanistic insights into Mps1 kinase activation. J Cell Mol Med. 2009, 13(8B): 1679-94.

Sun J#, Yu EY#, Yang Y, Confer LA, Sun SH, Wan K, Lue NF*, and Lei M* Stn1-Ten1 is an Rpa2-Rpa3-like complex at telomeres. Genes Dev. 2009, 23(24): 2900-14.

Chen Y#, Yang Y, van Overbeek M, Donigian JR, Baciu P, de Lange T, and Lei M* A shared docking motif in TRF1 and TRF2 used for differential recruitment of telomeric proteins. Science. 2008, 319(5866): 1092-6.

Wang F#, Podell ER, Zaug AJ, Yang Y, Baciu P, Cech TR, and Lei M* The POT1-TPP1 telomere complex is a telomerase processivity factor. Nature. 2007, 445(7127): 506-10.

Chen Y#, Yang Y, Wang F, Wan K, Yamane K, Zhang Y, and Lei M* Crystal structure of human histone lysine-specific demethylase 1 (LSD1). Proc Natl Acad Sci U S A. 2006, 103(38): 13956-61.