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


Journal

Epigenetics
ISSN: 1559-2308
Titre abrégé: Epigenetics
Pays: United States
ID NLM: 101265293

Informations de publication

Date de publication:
03 2020
Historique:
pubmed: 13 9 2019
medline: 22 4 2021
entrez: 13 9 2019
Statut: ppublish

Résumé

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.

Identifiants

pubmed: 31512982
doi: 10.1080/15592294.2019.1664229
pmc: PMC7028344
doi:

Substances chimiques

DNA-Binding Proteins 0
Histones 0
MSN2 protein, S cerevisiae 0
MSN4 protein, S cerevisiae 0
Mediator Complex 0
NUT1 protein, S cerevisiae 0
Saccharomyces cerevisiae Proteins 0
Transcription Factors 0
Histone Acetyltransferases EC 2.3.1.48
Sas2 protein, S cerevisiae EC 2.3.1.48
HOG1 protein, S cerevisiae EC 2.7.11.24
Mitogen-Activated Protein Kinases EC 2.7.11.24

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

251-271

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Auteurs

María E Pérez-Martínez (ME)

Departament de Bioquímica i Biologia Molecular and ERI Biotecmed, Universitat de València, Burjassot, Spain.

Marta Benet (M)

Departament de Bioquímica i Biologia Molecular and ERI Biotecmed, Universitat de València, Burjassot, Spain.

Paula Alepuz (P)

Departament de Bioquímica i Biologia Molecular and ERI Biotecmed, Universitat de València, Burjassot, Spain.

Vicente Tordera (V)

Departament de Bioquímica i Biologia Molecular and ERI Biotecmed, Universitat de València, Burjassot, Spain.

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