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

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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.
Publisher
KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
Issue Date
2015-01
Language
English
Article Type
Article
Keywords

KAPPA-B-ALPHA; LIGASE; MECHANISM; HELICASE; PROTEIN; CHAINS; LYSINE

Citation

BMB REPORTS, v.48, no.1, pp.25 - 29

ISSN
1976-6696
DOI
10.5483/BMBRep.2015.48.1.057
URI
http://hdl.handle.net/10203/198256
Appears in Collection
BS-Journal Papers(저널논문)
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