Prof. William Chong Hang CHAO - Faculty of Health Sciences (FHS)

lornachau Chau Long Lei2022-09-02T16:04:29+08:002019-11-29|

Contact Information

Title

Associate Professor

Office

(Office) E12-3026 / (Lab) N22-4003

Phone

(Office) +853 8822 4908 / (Lab) +853 8822 2934

Fax

+853 8822 2314

Email

williamchao@um.edu.mo

Consultation Hours

Tue, Fri 14:15 – 15:15

Teaching

Course Outlines

HSCI1002 Introduction to Biological Sciences

HSCI7002 Biomedical Sciences

HSCI8005 Critical Scientific Reading, Writing and Analysis

Research Team

Name	Position	Office	Phone	Email
Qiuyun YAN	PhD Student (Lab Representative)	N22-4003	+853 8822 2934	yc17602@um.edu.mo
Haoweng WU	PhD Student	N22-4003	+853 8822 2934
Huadong LI	PhD Student	N22-4003	+853 8822 2934
Meilin WANG	PhD Student	N22-4003	+853 8822 2934

Education
PhD	The Institute of Cancer Research, University of London, United Kingdom (2011)
MBiochem	Molecular and Cellular Biochemistry, St Peter’s College, University of Oxford, United Kingdom (2007)

Position
09/2017 – Present	Associate Professor, Faculty of Health Sciences, University of Macau
2012 – 2017	Cancer Research UK Additional Quota Fellow, London Research Institute / The Francis Crick Institute, London
2011 – 2012	Postdoctoral 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.

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

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
2012	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

Grants
01/2019 – 12/2021	Structural studies of the cohesin ring opening mechanism (MYRG2018-00221-FHS)
10/2018 – 10/2021	Structural studies of circadian clock and cell cycle coupling via the Timeless protein (FDCT 0009/2018/A1)