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Arabidopsis RPD3-like histone deacetylases form multiple complexes involved in stress response
- Source :
- Journal of genetics and genomics = Yi chuan xue bao. 48(5)
- Publication Year :
- 2021
-
Abstract
- The Arabidopsis thaliana RPD3-type histone deacetylases have been known to form conserved SIN3-type histone deacetylase complexes, but whether they form other types of complexes is unknown. Here, we perform affinity purification followed by mass spectrometry and demonstrate that the Arabidopsis RPD3-type histone deacetylases HDA6 and HDA19 interact with several previously uncharacterized proteins, thereby forming three types of plant-specific histone deacetylase complexes, which we named SANT, ESANT, and ARID. RNA-seq indicates that the newly identified components function together with HDA6 and HDA19 and coregulate the expression of a number of genes. HDA6 and HDA19 were previously thought to repress gene transcription by histone deacetylation. We find that the histone deacetylase complexes can repress gene expression via both histone deacetylation-dependent and -independent mechanisms. In the mutants of histone deacetylase complexes, the expression of a number of stress-induced genes is up-regulated, and several mutants of the histone deacetylase complexes show severe retardation in growth. Considering that growth retardation is thought to be a trade-off for an increase in stress tolerance, we infer that the histone deacetylase complexes identified in this study prevent overexpression of stress-induced genes and thereby ensure normal growth of plants under nonstress conditions.
- Subjects :
- Arabidopsis
Biology
Histone Deacetylases
Histones
03 medical and health sciences
0302 clinical medicine
Transcription (biology)
Gene Expression Regulation, Plant
Stress, Physiological
Heterochromatin
Gene expression
Protein Interaction Mapping
Genetics
Arabidopsis thaliana
Gene Silencing
Protein Interaction Maps
Molecular Biology
030304 developmental biology
0303 health sciences
Gene Expression Profiling
Computational Biology
Acetylation
biology.organism_classification
Cell biology
Histone
Phenotype
Multiprotein Complexes
Histone deacetylase complex
biology.protein
Histone deacetylase
030217 neurology & neurosurgery
Subjects
Details
- ISSN :
- 16738527
- Volume :
- 48
- Issue :
- 5
- Database :
- OpenAIRE
- Journal :
- Journal of genetics and genomics = Yi chuan xue bao
- Accession number :
- edsair.doi.dedup.....77733b79e806721c42c736ad324f93a4