Proteasomal degradation of Sfp1 contributes to the repression of ribosome biogenesis during starvation and is mediated by the proteasome activator Blm10

Antonio Diaz Lopez, Krisztina Tar, Undine Krügel, Thomas Dange, Ignacio Guerrero Ros, Marion Schmidt

Research output: Contribution to journalArticle

27 Scopus citations

Abstract

The regulation of ribosomal protein (RP) gene transcription is tightly linked to the nutrient status of the cell and is under the control of metabolic signaling pathways. In Saccharomyces cerevisiae several transcriptional activators mediate efficient RP gene transcription during logarithmic growth and dissociate from RP gene promoters upon nutrient limitation. Repression of RP gene transcription appears to be regulated predominantly by posttranslational modification and cellular localization of transcriptional activators. We report here that one of these factors, Sfp1, is degraded by the proteasome and that the proteasome activator Blm10 is required for regulated Sfp1 degradation. Loss of Blm10 results in the stabilization and increased nuclear abundance of Sfp1 during nutrient limitation, increased transcription of RP genes, increased levels of RPs, and decreased rapamycin-induced repression of RP genes. Thus we conclude that proteasomal degradation of Sfp1 is mediated by Blm10 and contributes to the repression of ribosome biogenesis under nutrient depletion.

Original languageEnglish (US)
Pages (from-to)528-540
Number of pages13
JournalMolecular biology of the cell
Volume22
Issue number5
DOIs
StatePublished - Mar 1 2011

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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