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(2) Kinetic and Protein-Protein Interaction Studies of Human DNA Polymerases lambda, µ and TdT

The DNA in every cell of the human body is spontaneously damaged more than 10,000 times every day. DNA repair plays a major role to maintain genome integrity in cells. Human DNA polymerase l discovered recently shares sequence similarity with the well-known DNA repair polymerase b and is thereby believed to catalyze base-excision repair. Human DNA polymerase µ also discovered recently shares sequence and functions similarity with the well-known human deoxynucleotidyl transferase (TdT) which involves in antibody generation. My group has purified the three X-family polymerases and is characterizing them kinetically. In addition, the three enzymes have N-terminal BRCT domain which supposedly interacts with cell-cycle checking proteins, such as the tumor suppressor p53. We are trying to identify these interacting proteins by employing immuno-precipitation assay and mass spectroscopy analysis. Moreover, we are trying to crystallize both lambda and mu in the presence of DNA and dNTP substrates in the collaboration with the Todd Yeates's group at UCLA.

(1) Pre-Steady State Kinetic Studies of DNA Lesion Bypass Polymerases

(2) Kinetic and Protein-Protein Interaction Studies of Human DNA Polymerases l, µ and TdT

(3) Mechanistic Studies of Vaccinia Virus DNA Polymerases and Design/Synthesis of Novel Nucleoside Analog Inhibitors

(4) Design and Synthesis of Novel Nucleoside Analog Inhibitors

(5) Developing Anti-HCV Peptide-Based Inhibitors

(6) Effects of HCV Protease NS3/4A on Human Kinases Involved in Immune Response