Different Modes of Action of Genetic and Chemical Downregulation of Histone Deacetylases with Respect to Plant Development and Histone Modifications

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Authors

LOCHMANOVÁ Gabriela IHNATOVÁ Ivana KUCHAŘÍKOVÁ Hana BRABENCOVÁ Sylva ZACHOVÁ Dagmar FAJKUS Jiří ZDRÁHAL Zbyněk FOJTOVÁ Miloslava

Year of publication 2019
Type Article in Periodical
Magazine / Source INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
MU Faculty or unit

Central European Institute of Technology

Citation
Web https://www.mdpi.com/1422-0067/20/20/5093
Doi http://dx.doi.org/10.3390/ijms20205093
Keywords Arabidopsis thaliana; epigenetics; histone; mass spectrometry; post-translational modifications; sodiumbutyrate; trichostatin A
Description A high degree of developmental plasticity enables plants to adapt to continuous, often unfavorable and unpredictable changes in their environment. At the molecular level, adaptive advantages for plants are primarily provided by epigenetic machinery including DNA methylation, histone modifications, and the activity of noncoding RNA molecules. Using a mass spectrometry-based proteomic approach, we examined the levels of acetylated histone peptide forms in Arabidopsis plants with a loss of function of histone deacetylase 6 (HDA6), and in plants germinated in the presence of HDA inhibitors trichostatin A (TSA) and sodium butyrate (NaB). Our analyses revealed particular lysine sites at histone sequences targeted by the HDA6 enzyme, and by TSA- and NaB-sensitive HDAs. Compared with plants exposed to drugs, more dramatic changes in the overall profiles of histone post-translational modifications were identified in hda6 mutants. However, loss of HDA6 was not sufficient by itself to induce hyperacetylation to the maximum degree, implying complementary activities of other HDAs. In contrast to hda6 mutants that did not exhibit any obvious phenotypic defects, the phenotypes of seedlings exposed to HDA inhibitors were markedly affected, showing that the effect of these drugs on early plant development is not limited to the modulation of histone acetylation levels.
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