title: Interactome analysis of yeast glutathione peroxidase 3.
abstract: Oxidative stress damages all cellular constituents, and therefore, cell has to possess various defense mechanisms to cope. Saccharomyces cerevisiae, widely used as a model organism for studying cellular responses to oxidative stress, contains three glutathione peroxidase (Gpx) proteins. Among them, Gpx3 plays a major defense role against oxidative stress in S. cerevisiae. In this study, in order to identify the new interaction proteins of Gpx3, we carried out two-dimensional gel electrophoresis after immunoprecipitation (IP-2DE), and MALDI-TOF mass spectrometry. The results showed that several proteins including protein disulfide isomerase, glutaredoxin 2, and SSY protein 3 specifically interact with Gpx3. These findings led us to suggest the possibility that Gpx3, known as a redox sensor and ROS scavenger, has another functional role by interacting with several proteins with various cellular functions.
authors.affiliation: Translational Research Center, KRIBB, Daejeon 305-806, Korea.
authors.forename: Phil Young
authors.initials: PY
authors.lastname: Lee
authors.forename: Kwang-Hee
authors.initials: KH
authors.lastname: Bae
authors.forename: Chang Won
authors.initials: CW
authors.lastname: Kho
authors.forename: Sunghyun
authors.initials: S
authors.lastname: Kang
authors.forename: Do Hee
authors.initials: DH
authors.lastname: Lee
authors.forename: Sayeon
authors.initials: S
authors.lastname: Cho
authors.forename: Seongman
authors.initials: S
authors.lastname: Kang
authors.forename: Sang Chul
authors.initials: SC
authors.lastname: Lee
authors.forename: Byoung Chul
authors.initials: BC
authors.lastname: Park
authors.forename: Sung Goo
authors.initials: SG
authors.lastname: Park