Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0038187 (starvation)
 24,951 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The aminoacyl-tRNA synthetases are inactivated in extracts of Saccharomyces cerevisiae preferentially to other yeast enzymes and the rate of inactivation greatly increases in extracts of nitrogen-starved cells. The intensity of inactivation varies for the different synthetases. Under conditions in which more than 80 per cent of the leucyl and isoleucyl-tRNA synthetases are inactivated, the activities of the synthetases for serine and arginine remain unchanged and the synthetases for other amino acids are inactivated to different extents. We have analyzed the characteristics of inactivation of the leucyl-tRNA synthetase, and identified the inactivating agent as the yeast proteinase yscB by the following criteria: co-induction of both activities by nitrogen starvation; same pattern of sensitivity to yeast proteinase inhibitors; co-purification through a procedure designed to purify the proteinase yscB and lack of inactivating activity in extracts of a nitrogen-starved yeast mutant lacking proteinase yscB.
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PMID:Yeast proteinase yscB inactivates the leucyl tRNA synthetase in extracts of Saccharomyces cerevisiae. 201 74

Mutants deficient in the vacuolar (lysosomal) endopeptidases proteinase yscA and proteinase yscB of the yeast Saccharomyces cerevisiae exhibit a drastically reduced protein degradation rate under nutritional stress conditions. The differentiation process of sporulation is considerably disturbed by the absence of the two endopeptidases. Also under vegetative growth conditions and under conditions of false protein synthesis, the two vacuolar endopeptidases exhibit some effect on protein degradation, which is, however, much less pronounced as found under starvation conditions. Proteinase yscA deficiency leads to rapid cell death when glucose-grown cells starve for nitrogen or other nutrients. Whereas overall protein degradation is affected in the endopeptidase mutants, degradation of two distinct false proteins analyzed is not altered in the absence of proteinase yscA and proteinase yscB. Also catabolite inactivation and degradation of fructose-1,6-bisphosphatase is not affected to a greater extent in the endopeptidase-deficient strains.
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PMID:Lysosomal (vacuolar) proteinases of yeast are essential catalysts for protein degradation, differentiation, and cell survival. 267 23

Vacuoles prepared from yeast cells of Candida albicans were enriched in proteinase ycaB (EC 3.4.21.48) but not in aminopeptidase or beta-glucosidase. Proteinase ycaB, assayed in situ, increased 1.5-fold during starvation whereas aminopeptidase activity decreased by 25%. Proteinase ycaB increased a further 1.5-fold during germ-tube formation.
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PMID:The cellular location of proteases in Candida albicans. 330 84

The activation process of vacuolar proteinases in the yeast Saccharomyces cerevisiae via precursor maturation is initiated by the PRA1/PEP4 gene product, proteinase yscA. Chromosomal deletion of the PRA1/PEP4 locus leads to accumulation of inactive pro-proteinases in the vacuole. Nine active-site mutations of proteinase yscA have been constructed in vitro. All these mutations lead to the expression of proteinase yscA species in vivo that are inactive against the in vitro substrate hemoglobin and the in vivo substrates pro-proteinase yscB and pro-carboxypeptidase yscY. However, three active-site mutations in proteinase yscA sustained the precursor maturation of proteinase yscB and carboxypeptidase yscY after exchange of the genomic wild-type allele with the respective proteinase yscA mutant alleles. In contrast to yeast strains deleted in proteinase yscA, the respective mutants carry out all cellular functions that rely on a proteolytically active vacuole. This wild-type behaviour of proteinase yscA mutant cells is dependent on the presence of active proteinase yscB. Proteinase yscA and proteinase yscB are equally able to fulfil essential cellular functions. For instance, either proteinase is able to maintain viability under starvation. However, mature proteinase yscB is not stable in the absence of proteinase yscA. The wild-type-like conformation of proteolytically inactive mutant proteinase yscA proteins stabilizes mature proteinase yscB and thus enables continuous maturation of pro-proteinase yscB by active proteinase yscB. After inhibition of the proteolytic activity of proteinase yscB in these proteinase yscA mutants with phenylmethysulfonyl fluoride or deletion of the PRB1 gene, maturation of all zymogens investigated in the vacuole, including the proteinase yscA mutant proteins, is blocked. The proteolytic activities of the vacuole in such a strain can be regained, however, by introduction of a wild-type proteinase yscA gene allowing subsequent autocatalytic maturation of wild-type pro-proteinase yscA. This indicates that an initial self-activation process of proteinase yscA is necessary for the activation of vacuolar zymogens.
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PMID:Biogenesis of the yeast vacuole (lysosome). The use of active-site mutants of proteinase yscA to determine the necessity of the enzyme for vacuolar proteinase maturation and proteinase yscB stability. 762 61

Autophagocytosis is a starvation-induced process responsible for transport of cytoplasmic proteins to the vacuole. In Saccharomyces cerevisiae, autophagy is characterized by the phenotypic appearance of autophagic vesicles inside the vacuole of strains deficient in proteinase yscB. The AUT1 gene, essential for autophagy, was isolated by complementation of the sporulation deficiency of a diploid aut1-1 mutant strain by a yeast genomic library and characterized. AUT1 is located on the right arm of chromosome XIV, 10 kb from the centromere, and encodes a protein of 310 amino acids, with an estimated molecular weight of 36 kDa. Cells carrying a chromosomal deletion of AUT1 are defective in the starvation-induced bulk flow transport of cytoplasmic proteins to the vacuole. aut1 null mutant strains are completely viable but show decreased survival rates during starvation. Homozygous delta aut1 diploid cells fail to sporulate. The selective cytoplasm-to-vacuole transport of aminopeptidase I is blocked in logarithmically growing and in starved delta autl cells. Deletion of the AUT1 gene had no obvious influence on secretion, fluid phase endocytosis, or vacuolar protein sorting. This supports the idea of autophagocytosis as being a novel route transporting proteins from the cytoplasm to the vacuole.
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PMID:AUT1, a gene essential for autophagocytosis in the yeast Saccharomyces cerevisiae. 902 85

Autophagocytosis is a starvation-induced process, carrying proteins destined for degradation to the lysosome. In the yeast Saccharomyces cerevisiae, the autophagic process is visualized by the appearance of autophagic vesicles in the vacuoles of proteinase yscB-deficient strains during starvation. aut3-1 mutant cells which exhibit a block in the autophagic process have been isolated previously. By using the drastically reduced sporulation frequency of homozygous aut3-1 diploid cells, the AUT3 gene was cloned by complementation. The Aut3 protein consists of 897 amino acids. The amino-terminal part of the protein shows significant homologies to serine/threonine kinases. aut3 null mutant cells are fully viable on rich media but show a reduced survival rate upon starvation. They are unable to accumulate autophagic vesicles in the vacuole during starvation. Starvation-induced vacuolar protein breakdown is almost completely impaired in aut3-deficient cells. Vacuolar morphology and acidification are not influenced in aut3-deficient cells. Also, secretion of invertase, endocytic uptake of Lucifer Yellow, and vacuolar protein sorting appear wild type like in aut3-deficient cells, suggesting autophagocytosis as a novel route for the transport of proteins from the cytosol to the vacuole. By using a fusion of Aut3p with green-fluorescent protein, Aut3p was localized to the cytosol.
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PMID:AUT3, a serine/threonine kinase gene, is essential for autophagocytosis in Saccharomyces cerevisiae. 919 Aug 2