Nutritional upshift response of ribosomal protein gene transcription in Saccharomyces cerevisiae

Griffioen, G

doi:10.1016/0378-1097(94)90286-0

Cited by 22 publications

(41 citation statements)

References 21 publications

(32 reference statements)

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“…The ␤-galactosidase activity shifted from a low steady-state level to a higher steady-state level within the first 2 h; thereafter it remained constant. This pattern of expression is remarkably similar to the pattern of expression of ribosomal proteins after nutritional upshift (Griffioen et al, 1994). This result argues against the idea that the higher ␤-galactosidase level in rapidly growing cells is a response to ethanol stress.…”

supporting

confidence: 56%

Complex Regulation of the Yeast Heat Shock Transcription Factor

Bonner

Carlson

Fackenthal

et al. 2000

MBoC

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The yeast heat shock transcription factor (HSF) is regulated by posttranslational modification. Heat and superoxide can induce the conformational change associated with the heat shock response. Interaction between HSF and the chaperone hsp70 is also thought to play a role in HSF regulation. Here, we show that the Ssb1/2p member of the hsp70 family can form a stable, ATP-sensitive complex with HSF-a surprising finding because Ssb1/2p is not induced by heat shock. Phosphorylation and the assembly of HSF into larger, ATP-sensitive complexes both occur when HSF activity decreases, whether during adaptation to a raised temperature or during growth at low glucose concentrations. These larger HSF complexes also form during recovery from heat shock. However, if HSF is assembled into ATP-sensitive complexes (during growth at a low glucose concentration), heat shock does not stimulate the dissociation of the complexes. Nor does induction of the conformational change induce their dissociation. Modulation of the in vivo concentrations of the SSA and SSB proteins by deletion or overexpression affects HSF activity in a manner that is consistent with these findings and suggests the model that the SSA and SSB proteins perform distinct roles in the regulation of HSF activity. INTRODUCTIONIt has long been known that in cells of many species, including Escherichia coli and Saccharomyces cerevisiae, cell division rates are tightly coupled with the steady-state levels and rates of synthesis of ribosomal proteins and rRNA. For example, cells in rich media, with a short generation time, display higher abundance of rRNA and higher rates of synthesis of ribosomal proteins than do cells in poor media, with a long generation time. In E. coli, some of this regulation is achieved by transcriptional attenuation and translational regulation via binding of ribosomal proteins to the RNAs of target operons (Freedman et al., 1985;Cole and Nomura, 1986). In yeast, regulation is partly transcriptional, via RAP1 and its binding site, the upstream activating sequence (UAS) rpg (Herruer et al., 1987;Moehle and Hinnebusch, 1991;Kraakman et al., 1993), although much of the regulation of ribosomal protein abundance is achieved by a competition between the assembly into ribosomes and the rapid degradation of unassembled ribosomal proteins (Warner et al., 1985;Maicas et al., 1988).Growth rate control clearly modulates the level of the translational machinery, which in turn influences the overall rate of protein synthesis. Changes in the rates of protein synthesis must, in turn, have profound implications for the protein chaperone system. Newly synthesized polypeptides typically do not adopt their mature conformation immediately but instead follow a complex folding pathway. For many proteins, the cytoplasmic chaperone system plays an integral role in helping these polypeptides adopt their mature conformations (for review, see Hendrick and Hartl, 1995). The hsp70 proteins are generally believed to bind efficiently to nascent or newly synthesized polypeptides...

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supporting

confidence: 56%

Complex Regulation of the Yeast Heat Shock Transcription Factor

Bonner

Carlson

Fackenthal

et al. 2000

MBoC

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“…In contrast, it has been reported that these genes are still induced upon glucose addition in the presence of cycloheximide, demonstrating that this induction does not require ongoing protein synthesis (Griffioen et al, 1994). Together these observations provided an opportunity to test whether regulation of r-protein gene transcription by the TOR pathway requires protein synthesis.…”

Section: Repression Of R-protein Gene Expression By Rapamycin Does Nomentioning

confidence: 97%

“…Ribosomal protein gene expression is induced several fold when yeast cells grown on a nonfermentable carbon source, for example, ethanol or glycerol, are transferred to a glucose-containing medium (Kief and Warner, 1981;Kraakman et al, 1993;Griffioen et al, 1994). This induction appears to involve additional regulatory mechanisms that are distinct from those that function during steady-state growth (Griffioen et al, 1996).…”

Section: The Tor Pathway Is Required For R-protein Gene Induction In mentioning

confidence: 99%

Regulation of Ribosome Biogenesis by the Rapamycin-sensitive TOR-signaling Pathway inSaccharomyces cerevisiae

Powers

Walter

1999

MBoC

371

336

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The TOR (target of rapamycin) signal transduction pathway is an important mechanism by which cell growth is controlled in all eucaryotic cells. Specifically, TOR signaling adjusts the protein biosynthetic capacity of cells according to nutrient availability. In mammalian cells, one branch of this pathway controls general translational initiation, whereas a separate branch specifically regulates the translation of ribosomal protein (r-protein) mRNAs. InSaccharomyces cerevisiae, the TOR pathway similarly regulates general translational initiation, but its specific role in the synthesis of ribosomal components is not well understood. Here we demonstrate that in yeast control of ribosome biosynthesis by the TOR pathway is surprisingly complex. In addition to general effects on translational initiation, TOR exerts drastic control over r-protein gene transcription as well as the synthesis and subsequent processing of 35S precursor rRNA. We also find that TOR signaling is a prerequisite for the induction of r-protein gene transcription that occurs in response to improved nutrient conditions. This induction has been shown previously to involve both the Ras-adenylate cyclase as well as the fermentable growth medium–induced pathways, and our results therefore suggest that these three pathways may be intimately linked.

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“…PKA activates the transcription of ribosomal protein genes as well (Herruer et al 1987;Kraakman et al 1993;Griffioen et al 1994). It was reported that PKA promotes nuclear localization and binding of the transcriptional activator Sfp1 to the promoters of ribosomal protein genes (Marion et al 2004).…”

Section: Regulation Of the Camp-pka Pathwaymentioning

confidence: 99%

Life in the midst of scarcity: adaptations to nutrient availability in Saccharomyces cerevisiae

et al. 2010

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Cells of all living organisms contain complex signal transduction networks to ensure that a wide range of physiological properties are properly adapted to the environmental conditions. The fundamental concepts and individual building blocks of these signalling networks are generally well-conserved from yeast to man; yet, the central role that growth factors and hormones play in the regulation of signalling cascades in higher eukaryotes is executed by nutrients in yeast. Several nutrient-controlled pathways, which regulate cell growth and proliferation, metabolism and stress resistance, have been defined in yeast. These pathways are integrated into a signalling network, which ensures that yeast cells enter a quiescent, resting phase (G 0 ) to survive periods of nutrient scarceness and that they rapidly resume growth and cell proliferation when nutrient conditions become favourable again. A series of well-conserved nutrient-sensory protein kinases perform key roles in this signalling network: i.e. Snf1, PKA, Tor1 and Tor2, Sch9 and Pho85-Pho80. In this review, we provide a comprehensive overview on the current understanding of the signalling processes mediated via these kinases with a particular focus on how these individual pathways converge to signalling networks that ultimately ensure the dynamic translation of extracellular nutrient signals into appropriate physiological responses.

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Nutritional upshift response of ribosomal protein gene transcription in Saccharomyces cerevisiae

Cited by 22 publications

References 21 publications

Complex Regulation of the Yeast Heat Shock Transcription Factor

Complex Regulation of the Yeast Heat Shock Transcription Factor

Regulation of Ribosome Biogenesis by the Rapamycin-sensitive TOR-signaling Pathway inSaccharomyces cerevisiae

Life in the midst of scarcity: adaptations to nutrient availability in Saccharomyces cerevisiae

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