Synergistic effect of two E2 ubiquitin conjugating enzymes in SCFhFBH1 catalyzed polyubiquitination

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 ubiqu...

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Published inBMB reports Vol. 48; no. 1; pp. 25 - 29
Main Authors Kim, J.H., Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Republic of Korea, Choi, J.S., Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Republic of Korea, Kim, S., Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Republic of Korea, Kim, K., Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Republic of Korea, Myung, P.K., Chungnam National University, Daejeon, Republic of Korea, Park, S.G., Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Republic of Korea, Seo, Y.S., Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Republic of Korea, Park, B.C., Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Republic of Korea
Format Journal Article
LanguageEnglish
Published Korean Society for Biochemistry and Molecular Biology 01.01.2015
생화학분자생물학회
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ISSN1976-6696
1976-670X
DOI10.5483/BMBRep.2015.48.1.057

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Summary: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 SCFhFBH1 using biochemical fractionations and MALDI-TOF. Moreover, we showed that recombinant UbcH5a and Cdc34 synergistically stimulate SCFhFBH1 catalyzed polyubiquitination in vitro. These data may provide an important cue to understand the mechanism how the SCF complex efficiently polyubiquitinates target substrates.
Bibliography:A50
These authors made equal contributions.
G704-SER000001672.2015.48.1.005
ISSN:1976-6696
1976-670X
DOI:10.5483/BMBRep.2015.48.1.057