Histone H3 threonine 11 phosphorylation by Sch9 and CK2 regulates chronological lifespan by controlling the nutritional stress response.
Upon nutritional stress, the metabolic status of cells is changed by nutrient signaling pathways to ensure survival. Altered metabolism by nutrient signaling pathways has been suggested to influence cellular lifespan. However, it remains unclear how chromatin regulation is involved in this process. Here, we found that histone H3 threonine 11 ... phosphorylation (H3pT11) functions as a marker for nutritional stress and aging. Sch9 and CK2 kinases cooperatively regulate H3pT11 under stress conditions. Importantly, H3pT11 defective mutants prolonged chronological lifespan (CLS) by altering nutritional stress responses. Thus, the phosphorylation of H3T11 by Sch9 and CK2 links a nutritional stress response to chromatin in the regulation of CLS.
Mesh Terms:
Acetic Acid, Casein Kinase II, Cell Division, Chromatin, Culture Media, Gene Expression Regulation, Fungal, Glucose, Histones, Phosphorylation, Protein Processing, Post-Translational, Protein Subunits, Protein-Serine-Threonine Kinases, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Signal Transduction, Stress, Physiological, Threonine
Acetic Acid, Casein Kinase II, Cell Division, Chromatin, Culture Media, Gene Expression Regulation, Fungal, Glucose, Histones, Phosphorylation, Protein Processing, Post-Translational, Protein Subunits, Protein-Serine-Threonine Kinases, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Signal Transduction, Stress, Physiological, Threonine
Elife
Date: Dec. 25, 2017
PubMed ID: 29938647
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