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Inducible dissociation of SCF Met30 ubiquitin ligase mediates a rapid transcriptional response to cadmium
Author(s) -
Barbey Régine,
BaudouinCornu Peggy,
Lee Traci A,
Rouillon Astrid,
Zarzov Patrick,
Tyers Mike,
Thomas Dominique
Publication year - 2005
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7600556
Subject(s) - art history , humanities , art , library science , computer science
Activity of the Met4 transcription factor is antagonized by the SCF Met30 ubiquitin ligase by degradation‐dependent and degradation‐independent mechanisms, in minimal and rich nutrient conditions, respectively. In this study, we show that the heavy metal Cd 2+ over‐rides both mechanisms to enable rapid Met4‐dependent induction of metabolic networks needed for production of the antioxidant and Cd 2+ ‐chelating agent glutathione. Cd 2+ inhibits SCF Met30 activity through rapid dissociation of the F‐box protein Met30 from the holocomplex. In minimal medium, dissociation of SCF Met30 complex is sufficient to impair the methionine‐induced degradation of Met4. In rich medium, dissociation of the SCF Met30 complex is accompanied by a deubiquitylation mechanism that rapidly removes inhibitory ubiquitin moieties from Met4. Post‐translational control of SCF Met30 assembly by a physiological stress to allow rapid induction of a protective gene expression program represents a novel mode of regulation in the ubiquitin system.