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CHAO CHONG HANG ASSOCIATE PROFESSOR
Title : ASSOCIATE PROFESSOR
Institute: Faculty of Health Sciences
Research Fields: 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. 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.
Contact email: williamchao@um.edu.mo
Notes: --
CHAO CHONG HANG

Research Contents

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.

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