15170
김석희Assistant Professor

Seokhee Kim studied chemistry and earned his B.S. from Seoul National University, Korea, in 2001. He started his doctoral research at Princeton University with Dr. Daniel Kahne and received a Ph.D. in Chemistry and Chemical Biology from Harvard University in 2008. He moved to Massachusetts Institute of Technology to work with Dr. Robert T. Sauer as a postdoctoral associate/fellow, and plans to open a new lab at SNU in early 2014. 

Seokhee Kim combined approaches in enzymology, biochemistry, biophysics, bacterial genetics, and structural biology to study two different protein complexes that are critical for maintaining the cell envelope of Gram-negative bacteria, and therefore, may provide new targets or strategies for development of new antimicrobial drugs. In his doctoral research, he provided insights on how a protein complex may help a distinct class of membrane proteins to fold and insert in the bacterial outer membrane by obtaining an atomic-level snapshot of the central component of this molecular machinery and by uncovering the structural organization of their components. In his postdoctoral research, he showed that a cell-envelope protease implicated
in the degradation of potentially toxic misfolded proteins has a distinct molecular mechanism of activity regulation, which are associated with two major transformations of the molecular machine. His works on the two molecular machines were published in prominent scientific journals. 

His main research interest is on structure, function, and cellular roles of proteolytic enzymes or related factors that are of biological and medical importance. Because intracellular proteolysis can be a double-edged sword, intricate balance of activity or substrate specificity is required for proper cellular function. Main questions are what distinct regulatory features are implanted in molecular architecture, how their dysregulation affect activity and cellular physiology, and how other factors or molecules can modulate the activity. The information obtained in these studies may not only lead to the fundamental understanding of operational principles and physiological roles of proteins, but also help develop new strategies to exploit enzymes that are associated with bacterial pathogenesis and human diseases.

Education

Ph.D. Chemistry and Chemical Biology, Harvard University, USA, 2008

B.S. Chemistry, Seould National Univerity, Seoul, Korea, 2001


Research Experiences

Assistant Professor, Department of Chemistry, Seoul National University, Korea, 2014-present

Postdoctoral Associate/Fellow, MIT, USA, 2008-2013


Representative Publications

S. Kim, R.T. Sauer, “Distinct regulatory mechanisms balance DegP proteolysis to maintain cellular fitness during heat stress.” Genes Dev, accepted, 2014

S. Kim, R.T. Sauer, “Cage assembly of DegP protease is not required for substrate-dependent regulation of proteolytic activity or high-temperature cell survival.” Proc Natl Acad Sci USA, 2012, 109, 7263

S. Kim, R.A. Grant, R.T. Sauer, “Covalent linkage of distinct substrate degrons controls assembly and disassembly of DegP proteolytic cages.” Cell, 2011, 145, 67-78
C.L. Hagan*, S. Kim*, D. Kahne, “Reconstitution of outer membrane protein assembly from purified components.” Science, 2010, 328, 890-892 *These authors contributed equally

S. Kim, J.C. Malinverni, P. Sliz, T.J. Silhavy, S.C. Harrison, D. Kahne, “Structure and Function of an Essential Component of the Outer Membrane Protein Assembly Machine.” Science, 2007, 317, 961-964

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