作者: Astrid Rouillon , Régine Barbey , E.Elizabeth Patton , Mike Tyers , Dominique Thomas
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摘要: Saccharomyces cerevisiae SCFMet30 ubiquitin–protein ligase controls cell cycle function and sulfur amino acid metabolism. We report here that the complex mediates transcriptional repression of MET gene network by triggering degradation activator Met4p when intracellular S–adenosylmethionine (AdoMet) increases. This AdoMet-induced is dependent upon 26S proteasome function. Unlike Met4p, other components specific activation complexes are assembled upstream genes do not appear to be regulated at protein level. provide evidence interaction between F-box Met30p occurs irrespective level AdoMet, suggesting timing controlled its with complex. also demonstrate a short-lived protein, which localizes within nucleus. Furthermore, transcription MET30 AdoMet levels Thus appears control own regulating amount ubiquitin ligase.