title: Synergistic effect of two E2 ubiquitin conjugating enzymes in SCF(hFBH1) catalyzed polyubiquitination.
abstract: Ubiquitination is a post translational modification which mostly links with proteasome dependent protein degradation. This process has been known to play pivotal roles in the number of biological events including apoptosis, cell signaling, transcription and translation. Although the process of ubiquitination has been studied extensively, the mechanism of polyubiquitination by multi protein E3 ubiquitin ligase, SCF complex remains elusive. In the present study, we identified UbcH5a as a novel stimulating factor for poly-ubiquitination catalyzed by SCF(hFBH1) using biochemical fractionations and MALDI-TOF. Moreover, we showed that recombinant UbcH5a and Cdc34 synergistically stimulate SCF(hFBH1) catalyzed polyubiquitination in vitro. These data may provide an important cue to understand the mechanism how the SCF complex efficiently polyubiquitinates target substrates.
authors.affiliation: Targeted Gene Regulation Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon 305-333; Department of Functional Genomics, University of Science and Technology (UST), Daejeon 305-350, Korea.
authors.forename: Jeong-Hoon
authors.initials: JH
authors.lastname: Kim
authors.affiliation: Medical Proteomics Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon 305-333; College of Pharmacy, Chungnam National University, Daejeon 305-764, Korea.
authors.forename: Jin Sun
authors.initials: JS
authors.lastname: Choi
authors.affiliation: Targeted Medicine Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Chungbuk 363-883, Korea.
authors.forename: Sunhong
authors.initials: S
authors.lastname: Kim
authors.affiliation: Medical Proteomics Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon 305-333, Korea.
authors.forename: Kidae
authors.initials: K
authors.lastname: Kim
authors.affiliation: College of Pharmacy, Chungnam National University, Daejeon 305-764, Korea.
authors.forename: Pyung Keun
authors.initials: PK
authors.lastname: Myung
authors.affiliation: Medical Proteomics Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon 305-333, Korea.
authors.forename: Sung Goo
authors.initials: SG
authors.lastname: Park
authors.affiliation: Department of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 305-701, Korea.
authors.forename: Yeon-Soo
authors.initials: YS
authors.lastname: Seo
authors.affiliation: Medical Proteomics Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon 305-333, Korea.
authors.forename: Byoung Chul
authors.initials: BC
authors.lastname: Park
mesh_terms: D000595:Amino Acid Sequence; D055162:Biocatalysis; D006367:HeLa Cells; D006801:Humans; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics; D044843:SKP Cullin F-Box Protein Ligases / Q000378:metabolism*; D016415:Sequence Alignment; D044763:Ubiquitin-Conjugating Enzymes / Q000235:genetics / Q000378:metabolism*; D054875:Ubiquitination
chemical_list: D011994:Recombinant Proteins; C577447:CDC34 protein, human; C097308:UBE2D1 protein, human; C097310:UBE2D3 protein, human; D044763:Ubiquitin-Conjugating Enzymes; D044843:SKP Cullin F-Box Protein Ligases