title: Interplay among Gcn5, Sch9 and mitochondria during chronological aging of wine yeast is dependent on growth conditions.
abstract: Saccharomyces cerevisiae chronological life span (CLS) is determined by a wide variety of environmental and genetic factors. Nutrient limitation without malnutrition, i.e. dietary restriction, expands CLS through the control of nutrient signaling pathways, of which TOR/Sch9 has proven to be the most relevant, particularly under nitrogen deprivation. The use of prototrophic wine yeast allows a better understanding of the role of nitrogen in longevity in natural and more demanding environments, such as grape juice fermentation. We previously showed that acetyltransferase Gcn5, a member of the SAGA complex, has opposite effects on CLS under laboratory and winemaking conditions, and is detrimental under the latter. Here we demonstrate that integrity of the SAGA complex is necessary for prolonged longevity, as its dismantling by SPT20 deletion causes a drop in CLS under both laboratory and winemaking conditions. The sch9Δ mutant is long-lived in synthetic SC medium, as expected, and the combined deletion of GCN5 partially suppresses this phenotype. However it is short-lived in grape juice, likely due to its low nitrogen/carbon ratio. Therefore, unbalance of nutrients can be more relevant for life span than total amounts of them. Deletion of RTG2, which codes for a protein associated with Gcn5 and is a component of the mitochondrial retrograde signal, and which communicates mitochondrial dysfunction to the nucleus, is detrimental under laboratory, but not under winemaking conditions, where respiration seems not so relevant for longevity. Transcription factor Rgm1 was found to be a novel CLS regulator Sch9-dependently.
authors: Department of Biotechnology, Institute of Agrochemistry and Food Technology, IATA-CSIC, Paterna, Spain; Departament of Biochemistry and Molecular Biology, University of Valencia, Burjassot, Spain.
authors: Cecilia
authors: C
authors: Picazo
authors: Department of Biotechnology, Institute of Agrochemistry and Food Technology, IATA-CSIC, Paterna, Spain; Departament of Biochemistry and Molecular Biology, University of Valencia, Burjassot, Spain.
authors: Helena
authors: H
authors: Orozco
authors: Department of Biotechnology, Institute of Agrochemistry and Food Technology, IATA-CSIC, Paterna, Spain; Departament of Biochemistry and Molecular Biology, University of Valencia, Burjassot, Spain.
authors: Emilia
authors: E
authors: Matallana
authors: Department of Biotechnology, Institute of Agrochemistry and Food Technology, IATA-CSIC, Paterna, Spain.
authors: Agustín
authors: A
authors: Aranda
mesh_terms: D001343:Autophagy; D002467:Cell Nucleus / Q000378:metabolism; D010450:Endopeptidases / Q000235:genetics / Q000378:metabolism; D051548:Histone Acetyltransferases / Q000235:genetics* / Q000378:metabolism; D047908:Intracellular Signaling Peptides and Proteins / Q000172:deficiency / Q000235:genetics; D008136:Longevity; D008928:Mitochondria / Q000378:metabolism*; D009584:Nitrogen / Q000378:metabolism; D010641:Phenotype; D011494:Protein Kinases / Q000235:genetics* / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics* / Q000378:metabolism; D015398:Signal Transduction; D014157:Transcription Factors / Q000172:deficiency / Q000235:genetics; D014920:Wine / Q000382:microbiology*; D000099224:p300-CBP-Associated Factor
chemical_list: D010450:Endopeptidases; D051548:Histone Acetyltransferases; D047908:Intracellular Signaling Peptides and Proteins; D009584:Nitrogen; D011494:Protein Kinases; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; C079379:RTG2 protein, S cerevisiae; C099690:SPT20 protein, S cerevisiae; C501392:GCN5 protein, S cerevisiae; D000099224:p300-CBP-Associated Factor; C071569:SCH9 protein kinase; C503322:UBP8 protein, S cerevisiae