Sukyeong Lee, Ph.D.
Department of Biochemistry and Molecular Biology
Managing Director, X-ray Crystallography Facility
Education and Awards
- B.S., Chemistry, Seoul National University, South Korea
- M.Sc., Chemistry, Seoul National University, South Korea
- Ph.D., Biological Sciences, Purdue University, W. Lafayette, Indiana, 1997
- Postdoctoral, Biological Sciences, Purdue University, W. Lafayette, Indiana
- Postdoctoral, Molecular Biophysics and Biochemistry, Yale University/HHMI, New Haven, Connecticut
My research is focused on studying the structure, function, and mechanism of membrane-anchored AAA proteases using a multi-pronged approach combining structural studies (X-ray crystallography and electron microscope-based approaches) with biochemical, biophysical, and functional studies. AAA proteases are ubiquitously present in eubacteria as well as in mitochondria and chloroplasts of eukaryotic cells. In human, mutations in m-AAA protease cause distinct neurological disorders such as hereditary spastic paraplegia and SCA28. The goal of our research is to provide a detailed mechanistic understanding of AAA proteases in order to exploit this information for the design of new macromolecular machines with novel biological activities.
Figure adapted from M. Koppen and T. Langer. Crit. Rev. Biochem. Mol. Biol. 42, 221-242 (2007).
- Lee S, Augustin S, Tatsuta T, Gerdes F, Langer T, Tsai FT. Electron cryomicroscopy structure of a membrane-anchored mitochondrial AAA protease. J Biol Chem. 2011 Feb 11;286(6):4404-11. [PubMed]
- Lee S, Sielaff B, Lee J, Tsai FT. CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation. Proc Natl Acad Sci U S A. 2010 May 4;107(18):8135-40. [PubMed]
- Augustin S, Gerdes F, Lee S, Tsai FT, Langer T, Tatsuta T. An intersubunit signaling network coordinates ATP hydrolysis by m-AAA proteases. Mol Cell. 2009 Sep 11;35(5):574-85. [PubMed]
- Lee S, Choi JM, Tsai FT. Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB. Mol Cell. 2007 Jan 26;25(2):261-71. [PubMed]
- Rees I, Lee S, Kim H, Tsai FT. The E3 ubiquitin ligase CHIP binds the androgen receptor in a phosphorylation-dependent manner. Biochim Biophys Acta. 2006 Jun;1764(6):1073-9. [PubMed]
- Lee S, Sowa ME, Choi JM, Tsai FT. The ClpB/Hsp104 molecular chaperone-a protein disaggregating machine. J Struct Biol. 2004 Apr-May;146(1-2):99-105. [PubMed]
- Lee S, Sowa ME, Watanabe YH, Sigler PB, Chiu W, Yoshida M, Tsai FT. The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state. Cell. 2003 Oct 17;115(2):229-40. [PubMed]