Education / Career
2009.08. Bachelor, Department of Biological Sciences, College of Natural Sciences, Seoul National University
Research Interests
1. Specifying interacting regions between Sec61 and Sec63, major ER translocon components
In yeast endoplasmic reticulum (ER), an evolutionarily conserved peptide-conducting channel called the Sec complex performs translocation and membrane insertion of many protein substrates. The Sec complex consists of the Sec61 complex and the Sec63 complex, but exact region of their interaction has not been specified. We found that residues in the 2nd transmembrane domain of Sec61 are in close proximity with Sec63 by site-specific cross-linking method. We aim to pin-point interacting residues both in Sec61 and Sec63
2. Distinct roles and the complex formation of Ssh1, the Sec61 homolog
Ssh1 (Sec sixty-one homolog 1) complex in yeast ER membrane has been regarded as a subsidiary translocon complex redundant to the Sec61 complex. We have discovered a novel interaction between Ssh1 and Sec63, a key subunit required for protein translocation. As Sec61 and its homolog, Ssh1, share many of the Sec complex subunits, we are focusing on stoichiometric balance among Sec subunits and the distinct roles of the Ssh1 complex.
3. Characterization of a novel yeast protein YER053C-A
YER053C-A is a small transmembrane protein found in yeast ER and its interaction with Sec complex subunits has been reported by high-throughput studies. We, for the first time, provided biochemical evidences that YER053C-A interacts with Sec63, one of the major Sec complex subunits. We plan to explain biological roles of YER053C-A which is critical for cell survival under stressed conditions.
In yeast endoplasmic reticulum (ER), an evolutionarily conserved peptide-conducting channel called the Sec complex performs translocation and membrane insertion of many protein substrates. The Sec complex consists of the Sec61 complex and the Sec63 complex, but exact region of their interaction has not been specified. We found that residues in the 2nd transmembrane domain of Sec61 are in close proximity with Sec63 by site-specific cross-linking method. We aim to pin-point interacting residues both in Sec61 and Sec63
2. Distinct roles and the complex formation of Ssh1, the Sec61 homolog
Ssh1 (Sec sixty-one homolog 1) complex in yeast ER membrane has been regarded as a subsidiary translocon complex redundant to the Sec61 complex. We have discovered a novel interaction between Ssh1 and Sec63, a key subunit required for protein translocation. As Sec61 and its homolog, Ssh1, share many of the Sec complex subunits, we are focusing on stoichiometric balance among Sec subunits and the distinct roles of the Ssh1 complex.
3. Characterization of a novel yeast protein YER053C-A
YER053C-A is a small transmembrane protein found in yeast ER and its interaction with Sec complex subunits has been reported by high-throughput studies. We, for the first time, provided biochemical evidences that YER053C-A interacts with Sec63, one of the major Sec complex subunits. We plan to explain biological roles of YER053C-A which is critical for cell survival under stressed conditions.
Publications
- Johannes H. Reithinger, Chewon Yim, Sungmin Kim, Hunsang Lee, and Hyun Kim,, "Structural and functional profiling of the lateral gate of the Sec61 translocon," J. Biol. Chem., 289(22), 15845-15855(2014).