Nut1/Hos1 and Sas2/Rpd3 control the H3 acetylation of two different sets of osmotic stress-induced genes

Epigenetics. 2020 Mar;15(3):251-271. doi: 10.1080/15592294.2019.1664229. Epub 2019 Sep 12.

Abstract

Epigenetic information is able to interact with the cellular environment and could be especially useful for reprograming gene expression in response to a physiological perturbation. In fact the genes induced or repressed by osmotic stress undergo significant changes in terms of the levels of various histone modifications, especially in the acetylation levels of histone H3. Exposing yeast to high osmolarity results in the activation of stress-activated protein kinase Hog1, which plays a central role in gene expression control. We evaluated the connection between the presence of Hog1 and changes in histone H3 acetylation in stress-regulated genes. We found a parallel increase in the acetylation of lysines 9 and 14 of H3 in induced genes during stress, which was largely dependent on Hog1 at the genome-wide level. Conversely, we observed that acetylation decreased in repressed genes and was not dependent on Hog1. However, lack of Hog1 sometimes produced different, and even opposite, effects on the induction and acetylation of H3 of each gene. We also found that the acetylation state of lysine 9 of H3 was altered in the strains deficient in Nut1 HAT and Hos1 HDAC in the genes up-regulated during osmotic stress in an Msn2/Msn4-independent manner, while lysine 9 acetylation of H3 varied in the strains deficient in Sas2 HAT and Rpd3 HDAC for the Msn2/Msn4-dependent induced genes. The results presented here show new, unexpected participants in gene regulation processes in response to environmental perturbations.

Keywords: Histone acetylation; chip-on-chip; chromatin; epigenetics; gene regulation; hog1; osmotic stress.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism
  • Epigenesis, Genetic
  • Gene Expression Regulation, Fungal*
  • Histone Acetyltransferases / genetics
  • Histone Acetyltransferases / metabolism*
  • Histone Code
  • Histones / metabolism*
  • Mediator Complex / genetics
  • Mediator Complex / metabolism*
  • Mitogen-Activated Protein Kinases / genetics
  • Mitogen-Activated Protein Kinases / metabolism
  • Osmotic Pressure*
  • Protein Processing, Post-Translational*
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Transcription Factors / genetics
  • Transcription Factors / metabolism

Substances

  • DNA-Binding Proteins
  • Histones
  • MSN2 protein, S cerevisiae
  • MSN4 protein, S cerevisiae
  • Mediator Complex
  • NUT1 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Histone Acetyltransferases
  • Sas2 protein, S cerevisiae
  • HOG1 protein, S cerevisiae
  • Mitogen-Activated Protein Kinases

Grants and funding

This work has been supported by grants from the Spanish MiNECO (BFU2013-48643-C3-3-P & BFU2016-77728-C3-3-P) to J.E. Pérez Ortín and P. Alepuz, from the Regional Valencian Government (Generalitat Valenciana) (PROMETEO II 2015/006) to J.E. Pérez Ortín, and from Universitat de València (UV-INV-AE13-139034) to P. Alepuz. M.E. Pérez-Martínez was supported by a grant (BES-2014-070587) of FPI from the Spanish MiNECO. The authors received support from European Union funds (FEDER);Generalitat Valenciana[BFU2013-48643-C3-3-P & BFU2016-77728-C3-3-P];Universitat de València [UV-INV-AE13-139034];