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 in | BMB reports Vol. 48; no. 1; pp. 25 - 29 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Korean Society for Biochemistry and Molecular Biology
01.01.2015
생화학분자생물학회 |
Subjects | |
Online Access | Get full text |
ISSN | 1976-6696 1976-670X |
DOI | 10.5483/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. |
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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 |