Contact Information
Address(Office)E12-3026
(Lab)N22-4004
Phone(Office)8822 4908
(Lab)8822 2935
Fax8822 2314
Emailwilliamchao@um.edu.mo
Laboratory Websitehttps://williamchao.wixsite.com/williamchaolab
Education
Ph.D.The Institute of Cancer Research, London, United Kingdom (2011)
MBiochem (Hons)Molecular and Cellular Biochemistry, St Peter’s College, University of Oxford, United Kingdom (2007)
Position
2017.9.18-presentAssociate Professor, Faculty of Health Sciences, University of Macau
2012-2017Cancer Research UK Additional Quota Fellow, London Research Institute / The Francis Crick Institute, London
2011-2012Postdoctoral Fellow, The Institute of Cancer Research, London
Research Interests
The remarkable accuracy of eukaryotic cell division is maintained by the cohesin-mediated entrapment of sister chromatids. The topological entrapment of DNA relies on the opening of the cohesin ring, which is stimulated by the Scc2-Scc4 loader complex.

A substantial amount of genetic and biochemical data has recently been generated to help explain the cohesin ring opening mechanism. Yet there is still much debate about the exact region in cohesin for DNA to enter. Most importantly, the structural information that can define the molecular gymnastics of how Scc2-Scc4 opens the cohesin ring is still missing.

To obtain such important information, my laboratory will apply X-ray crystallography and cryo-electron microscopy (cryo-EM) to determine the structures of cohesin-regulator complexes with the aim to understand the cohesin ring opening mechanism. The acquired knowledge will allow the cancer research community to rationalise oncogenic protein mutations, potentially contributing to the understanding of cancer and other hereditary diseases.

Representative Publications
  • Chao, W.C.H.*, Wade, B.O.*, Bouchoux, C., Jones, A.W., Purkiss, A.G., Federico, S., O’Reilly, N., Snijders, A.P., Uhlmann, F., and Singleton, M.R. (2017). Structural basis of Eco1-mediated cohesin acetylation. Sci. Rep. 7:44313. doi:10.1038/srep44313
  • Sansregret, L., Patterson, J.O., Dewhurst, S., López-García, C., Koch, A., McGranahan, N., Chao, W.C.H., Barry, D.J., Rowan, A., Instrell, R., Horswell, S., Way, M., Howell, M., Singleton, M.R., Medema, R.H., Nurse, P., Petronczki, M., Swanton, C. (2017). APC/C dysfunction limits excessive cancer chromosomal instability. Cancer Discov. 7(2); 1–16
  • Chao, W.C.H., Murayama, Y., Muñoz, S., Jones, A.W., Wade, B.O., Purkiss, A.G., Hu, X.-W., Borg, A., Snijders, A.P., Uhlmann, F., Singleton, M.R. (2017). Structure of the cohesin loader Scc2. Nat. Commun 8, 13952.
  • Chao, W.C.H., Murayama, Y., Muñoz, S., Costa, A., Uhlmann, F., and Singleton, M.R. (2015). Structural studies reveal the functional modularity of the Scc2-Scc4 cohesin loader. Cell Rep. 12, 719–725.
  • Drosopoulos, K., Tang, C., Chao, W.C.H., and Linardopoulos, S. (2014). APC/C is an essential regulator of centrosome clustering. Nat. Commun. 5, 3686.
  • He, J.*, Chao, W.C.H.*, Zhang, Z., Yang, J., Cronin, N., and Barford, D. (2013). Insights into degron recognition by APC/C coactivators from the structure of an Acm1-Cdh1 complex. Mol. Cell 50, 649–660.
  • Ferguson, J.L., Chao, W.C.H., Lee, E., and Friedman, K.L. (2013). The anaphase promoting complex contributes to the degradation of the S. cerevisiae telomerase recruitment subunit Est1p. PLoS ONE 8, e55055.
  • Zhang, Z., Yang, J., Kong, E.H., Chao, W.C.H., Morris, E.P., da Fonseca, P.C.A., and Barford, D. (2013). Recombinant expression, reconstitution and structure of human anaphase-promoting complex (APC/C). Biochem. J. 449, 365–371.
  • Chao, W.C.H.*, Kulkarni, K.*, Zhang, Z., Kong, E.H., and Barford, D. (2012). Structure of the mitotic checkpoint complex. Nature 484, 208–213.
  • Brennan, D.F., Dar, A.C., Hertz, N.T., Chao, W.C.H., Burlingame, A.L., Shokat, K.M., and Barford, D. (2011). A Raf-induced allosteric transition of KSR stimulates phosphorylation of MEK. Nature 472, 366–369.*co-first authorships
Awards
  • Cancer Research UK Additional Quota Fellowship, London Research Institute, London, United Kingdom (2012)
  • Chairman’s Prize for Best PhD Student 2011, The Institute of Cancer Research, London, United Kingdom (2012)
Grants
  • MYRG2018-00221-FHS
  • FDCT_0009/2018/A1