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Department of Biochemistry and Molecular Biology

Houston, Texas

Images from biochemistry and molecular biology research
Verna and Marrs McLean Department of Biochemistry and Molecular Biology
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Sukyeong Lee, Ph.D.

Sukyeong Lee, Ph.D.

Assistant Professor
Department of Biochemistry and Molecular Biology

Managing Director, X-ray Crystallography Facility

slee@bcm.edu

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

Research Interests

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.

Low dose electron micrograph of a double-shelled rotavirus embedded in vitreous ice.

Figure adapted from M. Koppen and T. Langer. Crit. Rev. Biochem. Mol. Biol. 42, 221-242 (2007).

Selected Publications

  • 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]

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