ArticleThe Journal of biological chemistry2013
Yeast phospholipase C is required for normal acetyl-CoA homeostasis and global histone acetylation.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Dynamic global acetylation remodeling during the yeast heat shock response.Genome biology · 2026Article
- Oxidative Stress Induced by Lipotoxicity and Renal Hypoxia in Diabetic Kidney Disease and Possible Therapeutic Interventions: Targeting the Lipid Metabolism and Hypoxia.Antioxidants (Basel, Switzerland) · 2023Review
- Lipid metabolism in sickness and in health: Emerging regulators of lipotoxicity.Molecular cell · 2021Review
- Disruption in phosphate transport affects membrane lipid and lipid droplet homeostasis in Saccharomyces cerevisiae.Journal of bioenergetics and biomembranes · 2020Article
- De Novo Lipogenesis as a Source of Second Messengers in Adipocytes.Current diabetes reports · 2019Review
- Nuclear phosphoinositide regulation of chromatin.Journal of cellular physiology · 2018Review
- Yeast phospholipase C is required for stability of casein kinase I Yck2p and expression of hexose transporters.FEMS microbiology letters · 2017Article
- Functions for diverse metabolic activities in heterochromatin.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Protein acetylation in metabolism - metabolites and cofactors.Nature reviews. Endocrinology · 2016Review
- Protein acetylation and acetyl coenzyme a metabolism in budding yeast.Eukaryotic cell · 2014Review
- Histone hypoacetylation-activated genes are repressed by acetyl-CoA- and chromatin-mediated mechanism.Biochimica et biophysica acta · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Phospholipase C (Plc1p) is required for the initial step of inositol polyphosphate (InsP) synthesis, and yeast cells with deletion of the PLC1 gene are completely devoid of any InsPs and display aberrations in transcriptional regulation. Here we show that Plc1p is required for a normal level of histone acetylation; plc1Δ cells that do not synthesize any InsPs display decreased acetylation of bulk histones and global hypoacetylation of chromatin histones. In accordance with the role of Plc1p in supporting histone acetylation, plc1Δ mutation is synthetically lethal with mutations in several subunits of SAGA and NuA4 histone acetyltransferase (HAT) complexes. Conversely, the growth rate, sensitivity to multiple stresses, and the transcriptional defects of plc1Δ cells are partially suppressed by deletion of histone deacetylase HDA1. The histone hypoacetylation in plc1Δ cells is due to the defect in degradation of repressor Mth1p, and consequently lower expression of HXT genes and reduced conversion of glucose to acetyl-CoA, a substrate for HATs. The histone acetylation and transcriptional defects can be partially suppressed and the overall fitness improved in plc1Δ cells by increasing the cellular concentration of acetyl-CoA. Together, our data indicate that Plc1p and InsPs are required for normal acetyl-CoA homeostasis, which, in turn, regulates global histone acetylation.
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Registered trials
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