Synergistic effect of two E2 ubiquitin conjugating enzymes in SCFhFBH1 catalyzed polyubiquitination
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초록
Ubiquitination is a post translational modification whichmostly links with proteasome dependent protein degradation. This process has been known to play pivotal roles in thenumber of biological events including apoptosis, cellsignaling, transcription and translation. Although the processof ubiquitination has been studied extensively, the mechanismof polyubiquitination by multi protein E3 ubiquitin ligase, SCFcomplex remains elusive. In the present study, we identifiedUbcH5a as a novel stimulating factor for poly-ubiquitinationcatalyzed by SCFhFBH1 using biochemical fractionations andMALDI-TOF. Moreover, we showed that recombinant UbcH5aand Cdc34 synergistically stimulate SCFhFBH1 catalyzed polyubiquitinationin vitro. These data may provide an importantcue to understand the mechanism how the SCF complexefficiently polyubiquitinates target substrates.
Abstract
Ubiquitination is a post translational modification whichmostly links with proteasome dependent protein degradation. This process has been known to play pivotal roles in thenumber of biological events including apoptosis, cellsignaling, transcription and translation. Although the processof ubiquitination has been studied extensively, the mechanismof polyubiquitination by multi protein E3 ubiquitin ligase, SCFcomplex remains elusive. In the present study, we identifiedUbcH5a as a novel stimulating factor for poly-ubiquitinationcatalyzed by SCFhFBH1 using biochemical fractionations andMALDI-TOF. Moreover, we showed that recombinant UbcH5aand Cdc34 synergistically stimulate SCFhFBH1 catalyzed polyubiquitinationin vitro. These data may provide an importantcue to understand the mechanism how the SCF complexefficiently polyubiquitinates target substrates.
참고문헌 (17)
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