Efficient transcription of the glycolytic gene ADH1 and three translational component genes requires the GCR1 product, which can act through TUF/GRF/RAP binding sites.

Santangelo, George M.; Tornow, Joanne

doi:10.1128/mcb.10.2.859

Cited by 56 publications

(33 citation statements)

References 12 publications

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“…Not depicted in the figure are Bmh1 and Bmh2, the yeast homologues of 14-3-3 proteins, which have been shown recently to be involved in TOR signaling (Bertram et al, 1998). of many r-protein genes, as well as Gcr1, a protein required for the activity of both r-protein genes as well as genes involved in glycolysis (Santangelo and Tornow, 1990;Tornow et al, 1993). In support of possible involvement of Gcr1 in TOR signaling, we have observed that rapamycin also severely inhibits expression of several glycolytic genes, including ADH1, ENO1, and PGK1 (our unpublished results).…”

Section: Discussionmentioning

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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Section: Discussionmentioning

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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“…Not surprisingly, these are the genes most abundantly transcribed by RNA polymerase II in S. cerevisiae cultures growing rapidly on glucose; 26 of the 30 most highly expressed transcription units are in one of these two groups (392). Overall the Rap1 activation mechanism(s) accounts for 60 to 75% of RNA polymerase II transcription in rapidly growing cells (324,410).…”

Section: The Cell Cycle Connectionmentioning

confidence: 99%

“…Transcriptional activation by Rap1 was shown long ago to exhibit sensitivity to disruption of GCR1 (81,324,435). Genome-wide analysis has now demonstrated for the entire genome that genes with a Rap1 binding site in their promoter are also Gcr1 target genes (81,211,324,375,435).…”

Section: Transcriptional Induction Of Glycolytic and Ribosomal Proteimentioning

confidence: 99%

Glucose Signaling in Saccharomyces cerevisiae

Santangelo

2006

Microbiol Mol Biol Rev

479

481

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SUMMARY Eukaryotic cells possess an exquisitely interwoven and fine-tuned series of signal transduction mechanisms with which to sense and respond to the ubiquitous fermentable carbon source glucose. The budding yeast Saccharomyces cerevisiae has proven to be a fertile model system with which to identify glucose signaling factors, determine the relevant functional and physical interrelationships, and characterize the corresponding metabolic, transcriptomic, and proteomic readouts. The early events in glucose signaling appear to require both extracellular sensing by transmembrane proteins and intracellular sensing by G proteins. Intermediate steps involve cAMP-dependent stimulation of protein kinase A (PKA) as well as one or more redundant PKA-independent pathways. The final steps are mediated by a relatively small collection of transcriptional regulators that collaborate closely to maximize the cellular rates of energy generation and growth. Understanding the nuclear events in this process may necessitate the further elaboration of a new model for eukaryotic gene regulation, called “reverse recruitment.” An essential feature of this idea is that fine-structure mapping of nuclear architecture will be required to understand the reception of regulatory signals that emanate from the plasma membrane and cytoplasm. Completion of this task should result in a much improved understanding of eukaryotic growth, differentiation, and carcinogenesis.

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“…At the UAS of the glycolytic genes ENO1, TPI, and PYK1, Rap1p functions to promote the binding of Gcr1p, a protein that interacts with DNA only very weakly on its own (2,15,52). This could be achieved via a direct protein-protein interaction or by some effect of Rap1p on the surrounding DNA (44,51). There may also be some redundancy of function within the Nand C-terminal domains of Rap1p because it can promote DNA binding by Gcr1p in vitro as long as the DNA binding domain plus either the N terminus or the C terminus is present (33).…”

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confidence: 99%