The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses

Finley, Daniel; Özkaynak, Engin; Varshavsky, Alexander

doi:10.1016/0092-8674(87)90711-2

Cited by 824 publications

(570 citation statements)

References 62 publications

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“…However, analysis of hsp function in Saccharomyces cerevisiae has revealed that only a limited number of hsps have appreciable effects on the induction of thermotolerance during a conditioning heat shock (for a review, see Piper, 1993). In particular, Hsp104, Hsp70, Ctt1 and Ubi4 have been found to contribute to the acquisition of thermotolerance by promoting the resolubilization of aggregated proteins (Parsell et al, 1994), the sequestering and refolding of denatured proteins (for a review, see Mager and Ferreira, 1993), the prevention of oxidative damage (Wieser et al, 1991) and the proteolytic elimination of toxic proteins (Finley et al, 1987) respectively.…”

Section: Introductionmentioning

confidence: 99%

Trehalose synthesis is important for the acquisition of thermotolerance in Schizosaccharomyces pombe

Ribeiro

Reinders

Böller

et al. 1997

Molecular Microbiology

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SummaryYeast cells show an adaptive response to a mild heat shock, resulting in thermotolerance acquisition. This is accompanied by induction of heat-shock protein (hsp) synthesis and rapid accumulation of trehalose. Genetic approaches to determine the specific role of trehalose in heat-induced thermotolerance in Saccharomyces cerevisiae have been hampered by the finding that deletion of TPS1, the gene encoding trehalose-6-phosphate synthase, causes a variety of pleiotropic effects, including inability to grow on glucose-containing media. Here, we have studied a tps1 mutant of the yeast Schizosaccharomyces pombe that reportedly has no such growth defects. We show that tps1 mutants have a serious defect in heat shock-induced acquisition of thermotolerance if conditioned at highly elevated temperatures (40-42.5ЊC), which, in wild-type cells, prevent hsp but not trehalose synthesis. In contrast, hsp synthesis appears to become particularly important under conditions in which trehalose synthesis is either absent (in tps1 mutant strains) or not fully induced (conditioning at moderately elevated temperatures, i.e. 35ЊC). In addition, pka1 mutants deficient in cAMP-dependent protein kinase were examined. Unconditioned pka1 cells had low levels of trehalose but a high basal level of thermotolerance. It was found that pka1 mutant cells, contrary to wild-type cells, accumulated large amounts of trehalose, even during a 50ЊC treatment. pka1 tps1 double mutants lacked this ability and showed reduced intrinsic thermotolerance, indicating a particularly important role for trehalose synthesis, which takes place during the challenging heat shock.

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Section: Introductionmentioning

confidence: 99%

Trehalose synthesis is important for the acquisition of thermotolerance in Schizosaccharomyces pombe

Ribeiro

Reinders

Böller

et al. 1997

Molecular Microbiology

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“…Defective recovery of protein synthesis after heat-shock in the rsp5-1 mutant Under stress-conditions, like heat-shock, the UBI4 gene, which contains five repeats of the ubiquitin-coding region, is upregulated [21]. Failure to respond properly to stress conditions could contribute to the observed ubiquitin deficiency of the rsp5-1 mutant.…”

Section: Altered Ubiquitin Homeostasis In the Rsp5-1 Mutantmentioning

confidence: 99%

The HECT E3 ubiquitin ligase Rsp5 is important for ubiquitin homeostasis in yeast

Krsmanović

Kölling

2004

FEBS Letters

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The HECT E3 ubiquitin ligase Rsp5, a yeast member of the Nedd4 family, has been implicated in many different aspects of cell physiology. Here, we present evidence that Rsp5 function is important for ubiquitin homeostasis. Several observations suggest that ubiquitin is limiting in the rsp5-1 mutant. Reduced synthesis of ubiquitin appears to contribute to ubiquitin depletion. A transient inhibition of general protein synthesis is observed in a wildtype strain upon heat-shock. While the wildtype cells quickly recover from this transient arrest, the rsp5-1 cells remain arrested. This suggests that Rsp5 is important for recovery from heat-induced protein synthesis arrest. Our results suggest that rsp5 phenotypes should be interpreted with caution, since some of the phenotypes could be simply the result of ubiquitin limitation.

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“…The yeast strains in this study were derived from DF5 (Finley et al, 1987), except yeast strain Sua7-TAP (a kind gift from Dr. Tilman Borggrefe), which is described in Borggrefe et al (2001). Yeast strains from DF5 were manipulated as previously described (Sherman et al, 1986).…”

Section: Yeast Strainsmentioning

confidence: 99%

Nuclear Import of TFIIB Is Mediated by Kap114p, a Karyopherin with Multiple Cargo-binding Domains

Hodges

Leslie

Mosammaparast

et al. 2005

MBoC

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Nuclear import and export is mediated by an evolutionarily conserved family of soluble transport factors, the karyopherins (referred to as importins and exportins). The yeast karyopherin Kap114p has previously been shown to import histones H2A and H2B, Nap1p, and a component of the preinitiation complex (PIC), TBP. Using a proteomic approach, we have identified several potentially new cargoes for Kap114p. These cargoes include another PIC component, the general transcription factor IIB or Sua7p, which interacted directly with Kap114p. Consistent with its role as a Sua7p import factor, deletion of KAP114 led to specific mislocalization of Sua7p to the cytoplasm. An interaction between Sua7p and TBP was also detected in cytosol, raising the possibility that both Sua7p and TBP can be coimported by Kap114p. We have also shown that Kap114p possesses multiple overlapping binding sites for its partners, Sua7p, Nap1p, and H2A and H2B, as well as RanGTP and nucleoporins. In addition, we have assembled an in vitro complex containing Sua7p, Nap1p, and histones H2A and H2B, suggesting that this Kap may import several proteins simultaneously. The import of more than one cargo at a time would increase the efficiency of each import cycle and may allow the regulation of coimported cargoes. INTRODUCTIONIn eukaryotic cells the nucleocytoplasmic transport of most proteins and some RNAs is mediated by an evolutionarily conserved family of soluble transport factors, the karyopherins (also referred to as importins and exportins; reviewed in Weis, 2003;Harel and Forbes, 2004;Mosammaparast and Pemberton, 2004). After synthesis in the cytoplasm, most nuclear protein cargoes are bound by a member of the karyopherin family, through direct interaction with a nuclear localization sequence contained in the cargo protein. Transport through the nuclear pore complex occurs via transient interactions of the karyopherin with the NPC. Once in the nucleus, the karyopherin encounters a high concentration of RanGTP, which acts as a regulator of transport. Interaction of the karyopherin with RanGTP leads to dissociation of the karyopherin from its nuclear cargo (Weis, 2003;Harel and Forbes, 2004;Mosammaparast and Pemberton, 2004). In some circumstances, nuclear-binding partners of the cargo appear to also play a role in stimulating the dissociation of Kap and cargo (Senger et al., 1998;Lee and Aitchison, 1999;Pemberton et al., 1999). In yeast, there are 14 members of the karyopherin family, with Ͼ20 members in mammalian cells (Mosammaparast and Pemberton, 2004). Karyopherins appear to function in either nuclear import or nuclear export, with only two examples of a Kap that works in both directions (Weis, 2003;Harel and Forbes, 2004;Mosammaparast and Pemberton, 2004). In yeast, 11 members of the karyopherin family must import at least 1500 nuclear proteins, suggesting that each receptor must have many cargoes. To date specific transport receptor-cargo pairs have only been shown for ϳ30 cargoes; in addition the NLS sequences recognized by most Kaps is n...

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The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses

Cited by 824 publications

References 62 publications

Trehalose synthesis is important for the acquisition of thermotolerance in Schizosaccharomyces pombe

Trehalose synthesis is important for the acquisition of thermotolerance in Schizosaccharomyces pombe

The HECT E3 ubiquitin ligase Rsp5 is important for ubiquitin homeostasis in yeast

Nuclear Import of TFIIB Is Mediated by Kap114p, a Karyopherin with Multiple Cargo-binding Domains

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