Dual regulation of the expression of the polyubiquitin gene by cyclic AMP and heat shock in yeast.

Tanaka, Katsuyuki; Matsumoto, Kunihiro; Toh‐e, Akio

doi:10.1002/j.1460-2075.1988.tb02837.x

Cited by 129 publications

(65 citation statements)

References 38 publications

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“…Treatment with cycloheximide resulted in a strong induction of UBI4 (Fig. 3), as previously observed in Dictystelium discoideum, Aspergillus nidulans, and cyclic AMP-deficient yeast mutants (25,28,46). This response might reflect a mechanism designed to restore ubiquitin levels.…”

Section: Vol 23 2003 Ubiquitin and Translational Inhibition 9253supporting

confidence: 52%

Ubiquitin Depletion as a Key Mediator of Toxicity by Translational Inhibitors

Hanna

Leggett

Finley

2003

Molecular and Cellular Biology

197

205

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Cycloheximide acts at the large subunit of the ribosome to inhibit translation. Here we report that ubiquitin levels are critical for the survival of Saccharomyces cerevisiae cells in the presence of cycloheximide: ubiquitin overexpression confers resistance to cycloheximide, while a reduced ubiquitin level confers sensitivity. Consistent with these findings, ubiquitin is unstable in yeast (t 1/2 ‫؍‬ 2 h) and is rapidly depleted upon cycloheximide treatment. Cycloheximide does not noticeably enhance ubiquitin turnover, but serves principally to block ubiquitin synthesis. Cycloheximide also induces UBI4, the polyubiquitin gene. The cycloheximide-resistant phenotype of ubiquitin overexpressors is also characteristic of partial-loss-of-function proteasome mutants. Ubiquitin is stabilized in these mutants, which may account for their cycloheximide resistance. Previous studies have reported that ubiquitin is destabilized in the absence of Ubp6, a proteasome-associated deubiquitinating enzyme, and that ubp6 mutants are hypersensitive to cycloheximide. Consistent with the model that cycloheximide-treated cells are ubiquitin deficient, the cycloheximide sensitivity of ubp6 mutants can be rescued either by ubiquitin overexpression or by mutations in proteasome subunit genes. These results also show that ubiquitin wasting in ubp6 mutants is proteasome mediated. Ubiquitin overexpression rescued cells from additional translational inhibitors such as anisomycin and hygromycin B, suggesting that ubiquitin depletion may constitute a widespread mechanism for the toxicity of translational inhibitors.

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Section: Vol 23 2003 Ubiquitin and Translational Inhibition 9253supporting

confidence: 52%

Ubiquitin Depletion as a Key Mediator of Toxicity by Translational Inhibitors

Hanna

Leggett

Finley

2003

Molecular and Cellular Biology

197

205

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“…DISCUSSION cAMP has been proposed to be involved in cell cycle control in S. cerevisiae and is known to affect the activity of enzymes like trehalase and glycogen synthetase (22). However, with the exception of some heat shock genes (34,38), little information is available concerning its role in the control of gene expression. The results of this investigation show that the expression of the S. cerevisiae CTTJ gene, which codes for a cytoplasmic catalase, is controlled by the supply of essential nutrients available to the cell.…”

Section: Resultsmentioning

confidence: 99%

Control of Saccharomyces cerevisiae catalase T gene (CTT1) expression by nutrient supply via the RAS-cyclic AMP pathway.

Bissinger¹,

Wieser²,

Hamilton³

et al. 1989

Mol. Cell. Biol.

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In Saccharomyces cerevisiae, lack of nutrients triggers a pleiotropic response characterized by accumulation of storage carbohydrates, early Gl arrest, and sporulation of a/at diploids. This response is thought to be mediated by RAS proteins, adenylate cyclase, and cyclic AMP (cAMP)-dependent protein kinases. This study shows that expression of the S. cerevisiae gene coding for a cytoplasmic catalase T (CTTI) is controlled by this pathway: it is regulated by the availability of nutrients. For growth on STMD2%, cells grown on YPD2% plates or in liquid YPD2% were transferred to STMD2% (optical density at 600 nm, 1.0) and were incubated at 30°C for 36 h (after this period, all cells were arrested unbudded in early Gl). Synthetic a-factor (kindly provided by K; Nasmyth) was added in some experiments to a final concentration of 0. 1 p.g per ml of culture. Cells were grown and incubated on SM in the same way as on STMD2%. Strains bearing cdc mutations were pregrown at 23°C on YPD2% to an optical density at 600 nm of 2.5, and the cultures were divided, transferred to STMD2% in some experiments, and incubated for 5 h at 23 and 35°C on YPD2% or STMD2%, respectively, before being harvested.Enzyme activities. The specific activity of ,-galactosidase of crude extracts from yeast strains bearing a single-copy CTTI-lacZ fusion gene (36) integrated into the chromosomal URA3 locus (see Fig. 1) was assayed as described by Miller (26).

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“…In addition, the Ras-PKA pathway stimulates Gcn4 transcriptional activity in response to UV light and nutritional stress by increasing both the translation and the activity of Gcn4 (11). In contrast, PKA inhibits transcription of ADR1, ADH2, CTT1, SSA3, TPS2, and UBI4 (4,9,14,37,57), and it also reduces the transcriptional activity of Adr1 (9).…”

Section: Discussionmentioning

confidence: 99%

Yap, a Novel Family of Eight bZIP Proteins in Saccharomyces cerevisiae with Distinct Biological Functions

Fernandes

Rodrigues-Pousada

Struhl

1997

Molecular and Cellular Biology

295

316

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Saccharomyces cerevisiae contains eight members of a novel and fungus-specific family of bZIP proteins that is defined by four atypical residues on the DNA-binding surface. Two of these proteins, Yap1 and Yap2, are transcriptional activators involved in pleiotropic drug resistance. Although initially described as AP-1 factors, at least four Yap proteins bind most efficiently to TTACTAA, a sequence that differs at position ؎2 from the optimal AP-1 site (TGACTCA); further, a Yap-like derivative of the AP-1 factor Gcn4 (A239Q S242F) binds efficiently to the Yap recognition sequence. Molecular modeling suggests that the Yap-specific residues make novel contacts and cause physical constraints at the ؎2 position that may account for the distinct DNA-binding specificities of Yap and AP-1 proteins. To various extents, Yap1, Yap2, Yap3, and Yap5 activate transcription from a promoter containing a Yap recognition site. Yap-dependent transcription is abolished in strains containing high levels of protein kinase A; in contrast, Gcn4 transcriptional activity is stimulated by protein kinase A. Interestingly, Yap1 transcriptional activity is stimulated by hydrogen peroxide, whereas Yap2 activity is stimulated by aminotriazole and cadmium. In addition, unlike other yap mutations tested, yap4 (cin5) mutations affect chromosome stability, and they suppress the cold-sensitive phenotype of yap1 mutant strains. Thus, members of the Yap family carry out overlapping but distinct biological functions.

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Dual regulation of the expression of the polyubiquitin gene by cyclic AMP and heat shock in yeast.

Cited by 129 publications

References 38 publications

Ubiquitin Depletion as a Key Mediator of Toxicity by Translational Inhibitors

Ubiquitin Depletion as a Key Mediator of Toxicity by Translational Inhibitors

Control of Saccharomyces cerevisiae catalase T gene (CTT1) expression by nutrient supply via the RAS-cyclic AMP pathway.

Yap, a Novel Family of Eight bZIP Proteins in Saccharomyces cerevisiae with Distinct Biological Functions

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