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 language | English (US) |
|---|---|
| Pages (from-to) | 528-540 |
| Number of pages | 13 |
| Journal | Molecular Biology of the Cell |
| Volume | 22 |
| Issue number | 5 |
| DOIs | |
| State | Published - Mar 1 2011 |
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ASJC Scopus subject areas
- Molecular Biology
- Cell Biology
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Proteasomal degradation of Sfp1 contributes to the repression of ribosome biogenesis during starvation and is mediated by the proteasome activator Blm10. / Lopez, Antonio Diaz; Tar, Krisztina; Krügel, Undine; Dange, Thomas; Ros, Ignacio Guerrero; Schmidt, Marion.
In: Molecular Biology of the Cell, Vol. 22, No. 5, 01.03.2011, p. 528-540.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Proteasomal degradation of Sfp1 contributes to the repression of ribosome biogenesis during starvation and is mediated by the proteasome activator Blm10
AU - Lopez, Antonio Diaz
AU - Tar, Krisztina
AU - Krügel, Undine
AU - Dange, Thomas
AU - Ros, Ignacio Guerrero
AU - Schmidt, Marion
PY - 2011/3/1
Y1 - 2011/3/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=79952342817&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=79952342817&partnerID=8YFLogxK
U2 - 10.1091/mbc.E10-04-0352
DO - 10.1091/mbc.E10-04-0352
M3 - Article
C2 - 21209318
AN - SCOPUS:79952342817
VL - 22
SP - 528
EP - 540
JO - Molecular Biology of the Cell
JF - Molecular Biology of the Cell
SN - 1059-1524
IS - 5
ER -