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Qinghua Wang
wang0663@umn.edu
University of Science and Technology of China
Kylie Walters Lab
In the Walters lab, I am using NMR spectroscopy to solve the solution
structure of a C-terminal domain of the proteasome subunit S5a. S5a is
a component of the 19s regulatory complex of the 26s proteasome and has
been reported to bind polyubiquitin chains as well as the N-terminal
ubiquitin-like domain of hHR23a.
hHR23a is critical for DNA damage recognition and plays an
important role in both nucleotide excision
repair (NER) and base excision repair (BER). Additionally, hHR23a proteins
have recently been implicated in proteasome-mediated protein degradation.
The fragment of S5a that I am studying contains two ubiquitin binding
segments. After using triple resonance experiments to obtain the backbone
chemical shift assignments of S5a, I will map where hHR23a binds and study the
complex of these two proteins. This work will provide valuable insights
into the relationship between proteasome activity and DNA repair.
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