Regulation of transcription by ubiquitination without proteolysis: Cdc34/SCF(sup)Met30-mediated inactivation of the transcription factor Met4
Article Abstract:
Results show that the Cdc34 protein belonging to the SCF complex of enzymes is involved in the ubiquitation of transcription factors and functions independently of the proteolysis. Data also indicate that Met4 protein transcriptional repression and its ubiquitination are mediated by the Cdc34/SCF(sup)met30 complex.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2000
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Release of ubiquitin-charged Cdc34-S(squiggle)Ub from the RING domain is essential for ubiquitination of the SCF(sup)Cdc4-bound substrate Sic1
Article Abstract:
Research indicates that the formation of a ubiquitin thiol ester is involved in the regulation of Cdc34/SCF(sup)Cdc4 binding equilibrium in constrast to the view that RING domain bound Cdc34 ubiquitinates the substrate. Data show that release of ubiquitin-charged Cdc34-S(squiggle)Ub from the RING is a prerequisite for ubiquitination of the SCF(sup)Cdc4-bound Sic1 substrate.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2003
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Cdc34 and the F-box protein Met30 are required for degradation of the Cdk-inhibitory kinase Swe1
Article Abstract:
The F-box protein Met30 and Cdc23 are necessary for degradation of Swe1, a Cdk-inhibitory kinase based on recent work in Saccharomyces cerevisiae. Uniquitin-mediated proteolysis controls the abundance of many cell cycle regulatory proteins. A screen for genetic interactions with a cdc34 mutation found MET30, an essential gene for cell cycle progression. Extracts from cdc34 or met30 mutants are defective relative to polyubiquitination of Swe1.
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 1998
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