Suk-Hee Lee

Suk-Hee Lee, PhD

Professor of Biochemistry & Molecular Biology


Dr. Lee received a PhD in Microbiology from the University of Texas at Austin in 1987 in the laboratory of James R. Walker where his research focused on functional analysis of DNA polymerase III (Pol III) in E. coli and explored that the tau subunit of DNA Pol III possesses DNA-dependent ATPase activity. As a postdoc, he worked in the nucleic acid laboratory of Dr. Jerard Hurwitz at the Sloan-Kettering Cancer Center, NY, where he studied simian virus 40 (SV40) DNA replication in vitro, focusing on DNA polymerases delta and epsilon and their accessory factors to understand functions of DNA replicative polymerases in human. In 1992, he joined the faculty of the Virology and Molecular Biology department at St. Jude Children’s Research Hospital, Memphis, TN where his research areas include functional analysis of DNA pol III and human replication protein A (RPA), and regulation of DNA replication following DNA damage. Since joining the Department of Biochemistry & Molecular Biology at the IU School of Medicine in 1997, his work focused on the mechanism of DNA replication and repair in humans, including functional analysis of DNA polymerases alpha and delta, RPA, XPA, XPG, DNA-PK, and Ku70/80. Dr. Lee also focused on the role of two novel human proteins with exonuclease activity, Metnase (also known as SETMAR) and EEPD1. This work is in collaboration with investigators at the University of Florida School of Medicine and the Colorado State University. Metnase is a SET-transposase fusion protein that does not function as a classic transposase, but it uses biochemical properties of the SET and the transposase domains to promote non-homologous end-joining (NHEJ) repair and restart of stalled replication fork. EEPD1 has two N-terminal helix-hairpin-helix DNA binding domains related to RuvA, and a C-terminal DNase I-like domain in the exonuclease-endonuclease-phosphatase (EEP) family. Both Metnase and EEPD1 possess the 5’ endonuclease activity that enhances Exo1 nuclease activity at fork structures. His recent work explored that EEPD1 plays an essential role in initiating homologous recombination (HR) repair of stalled replication forks. 


(317) 278-3464 

635 Barnhill Drive Medical Science, Room MS406E
Indianapolis, IN 46202