Multilayered control of peroxisomal activity upon salt stress in Saccharomyces cerevisiae.
Peroxisomes are dynamic organelles and the sole location for fatty acid β-oxidation in yeast cells. Here, we report that peroxisomal function is crucial for the adaptation to salt stress, especially upon sugar limitation. Upon stress, multiple layers of control regulate the activity and the number of peroxisomes. Activated Hog1 MAP kinase triggers the induction of genes encoding enzymes for fatty acid activation, peroxisomal import and β-oxidation through the Adr1 transcriptional activator, which transiently associates with genes encoding fatty acid metabolic enzymes in a stress- and Hog1-dependent manner. Moreover, Na+and Li+stress increases the number of peroxisomes per cell in a Hog1-independent manner, which depends instead of the retrograde pathway and the dynamin related GTPases Dnm1 and Vps1. The strong activation of the Faa1 fatty acyl-CoA synthetase, which specifically localizes to lipid particles and peroxisomes, indicates that adaptation to salt stress requires the enhanced mobilization of fatty acids from internal lipid stores. Furthermore, the activation of mitochondrial respiration during stress depends on peroxisomes, mitochondrial acetyl-carnitine uptake is essential for salt resistance and the number of peroxisomes attached to the mitochondrial network increases during salt adaptation, which altogether indicates that stress-induced peroxisomal β-oxidation triggers enhanced respiration upon salt shock.
Instituto de Biomedicina de Valencia IBV-CSIC, Department of Molecular and Cellular Pathology and Therapy, Jaime Roig 11, Valencia, 46010, Spain.|Instituto de Biología Molecular y Celular de Plantas, CSIC-Universitat Politècnica de València, Ciudad Politécnica de la Innovación, Department of Biotechnology, Edificio 8E, Ingeniero Fausto Elio s/n, Valencia, 46022, Spain.
Sara
S
Manzanares-Estreder
Instituto de Biología Molecular y Celular de Plantas, CSIC-Universitat Politècnica de València, Ciudad Politécnica de la Innovación, Department of Biotechnology, Edificio 8E, Ingeniero Fausto Elio s/n, Valencia, 46022, Spain.
Joan
J
Espí-Bardisa
Instituto de Biomedicina de Valencia IBV-CSIC, Department of Molecular and Cellular Pathology and Therapy, Jaime Roig 11, Valencia, 46010, Spain.
Benito
B
Alarcón
Instituto de Biología Molecular y Celular de Plantas, CSIC-Universitat Politècnica de València, Ciudad Politécnica de la Innovación, Department of Biotechnology, Edificio 8E, Ingeniero Fausto Elio s/n, Valencia, 46022, Spain.
Amparo
A
Pascual-Ahuir
Instituto de Biomedicina de Valencia IBV-CSIC, Department of Molecular and Cellular Pathology and Therapy, Jaime Roig 11, Valencia, 46010, Spain.
Markus
http://orcid.org/0000-0002-6788-5830
M
Proft
D000214:Acyl Coenzyme A / Q000378:metabolism; D003066:Coenzyme A Ligases / Q000378:metabolism; D005227:Fatty Acids / Q000378:metabolism; D050356:Lipid Metabolism; D008055:Lipids / Q000096:biosynthesis; D008928:Mitochondria / Q000378:metabolism; D009997:Osmotic Pressure / Q000502:physiology; D010084:Oxidation-Reduction; D020675:Peroxisomes / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism; D012965:Sodium Chloride / Q000378:metabolism; D013312:Stress, Physiological / Q000502:physiology*
D000214:Acyl Coenzyme A; D005227:Fatty Acids; D008055:Lipids; D029701:Saccharomyces cerevisiae Proteins; D012965:Sodium Chloride; D003066:Coenzyme A Ligases