Arabidopsis thaliana
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA355037 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:We explore the genome-wide occupancy of 4 different chromatin regulating complexes encoded in S. cerevisiae. We provide the data for histone acetyltransferases Gcn5 and Esa1 and histone deacetylases Hst1 and Rpd3/Sin3 under rich growth condition (YPD medium). We also include the occupancy data for RNA polymerase II under the same growth condition.
2005-11-03 | E-WMIT-2 | biostudies-arrayexpress
Project description:Histone deacetylase inhibitor enhanced salinity stress response
| PRJNA292335 | ENA
Project description:Although the Arabidopsis thaliana RPD3-type histone deacetylases have been known to form SIN3 histone deacetylase complexes that are conserved in eukaryotes, it is unknown whether they also form other types of histone deacetylase complexes. Here, we performed affinity purification followed by mass spectrometry and demonstrated that the Arabidopsis RPD3-type histone deacetylases HDA6 and HDA19 can interact with several previously uncharacterized proteins and form three types of plant-specific histone deacetylase complexes, which we named SANT, ESANT, and ARID. RNA-seq indicated that HDA6 and HDA19 function together with other components of the histone deacetylase complexes and co-regulate the expression of a number of genes. HDA6 and HDA19 have been thought to repress gene transcription by histone deacetylation. We found that the histone deacetylase complexes can also repress gene expression via certain histone-deacetylation-independent mechanisms. In the mutants of the histone deacetylase complexes, the expression of a number of stress-induced genes was up-regulated. Several mutants of the histone deacetylase complexes showed severe retardation in growth. Considering that the growth retardation is thought to be a trade-off for the increase of stress tolerance, we predict that the histone deacetylase complexes identified in this study prevent overexpression of stress-induced genes and thereby ensure normal growth of plants under non-stress conditions.
2021-06-10 | GSE166089 | GEO
Project description:Although the Arabidopsis thaliana RPD3-type histone deacetylases have been known to form SIN3 histone deacetylase complexes that are conserved in eukaryotes, it is unknown whether they also form other types of histone deacetylase complexes. Here, we performed affinity purification followed by mass spectrometry and demonstrated that the Arabidopsis RPD3-type histone deacetylases HDA6 and HDA19 can interact with several previously uncharacterized proteins and form three types of plant-specific histone deacetylase complexes, which we named SANT, ESANT, and ARID. RNA-seq indicated that HDA6 and HDA19 function together with other components of the histone deacetylase complexes and co-regulate the expression of a number of genes. HDA6 and HDA19 have been thought to repress gene transcription by histone deacetylation. We found that the histone deacetylase complexes can also repress gene expression via certain histone-deacetylation-independent mechanisms. In the mutants of the histone deacetylase complexes, the expression of a number of stress-induced genes was up-regulated. Several mutants of the histone deacetylase complexes showed severe retardation in growth. Considering that the growth retardation is thought to be a trade-off for the increase of stress tolerance, we predict that the histone deacetylase complexes identified in this study prevent overexpression of stress-induced genes and thereby ensure normal growth of plants under non-stress conditions.
2021-06-10 | GSE166088 | GEO
Project description:Previous results suggest that Bmh might inhibit the activity of the transcription factor Adr1 after binding to Adr1-dependent promoters. In a strain lacking the two major histone deacetylases, Hda1 and Rpd3 (hdac?), Adr1 is bound to its target promoters recruiting what appears to be an inactive RNA ploymerase II preinitiation complex (PIC). To determine whether Bmh activity inhibits this inactive PIC and the generality of this effect on glucose-repressed gene expression, the mRNA profiles of wild type, bmh mutant, hdac mutant, and bmh hdac mutant cells grown in high glucose medium were compared. Total RNAs were purified from triplicate cultures of W303-1A (wild type), YLL1087 (bmh1-ts bmh2?), CTY-TY44 (hda1? rpd3?) and KBY3 (bmh1-ts bmh2? hda1? rpd3?) cells exponentially growing in YP broth containing 5% glucose and then profiled using Affymetrix Yeast 2.0 arrays.
2013-01-15 | E-GEOD-40116 | biostudies-arrayexpress
Project description:Class I histone deacetylases (HDAC) critically contribute to Ewing sarcoma pathogenesis II
| PRJNA683020 | ENA
Project description:Regulation of MIR165/166 by Class II and Class III homeodomain leucine zipper proteins establishes leaf polarity
| PRJNA275279 | ENA
Project description:Both of Histone Deacetylases HDA6 and HDA9 belong to RPD3/HDA1 class I subfamily, and they have similar protein structure. Loss of function of HDA9 display a blunt silique. Although there is not protein-protein interaction between HDA6 and HDA9, they simultaneously loss function led to “nock-shape” silique that more seriously silique phenotype than hda9. The silique valve cell of hda9 and hda6 hda9 were longer than wild type and hda6. The transcripts level of auxin signaling related genes were mis-regulated in hda9 and hda6 hda9 silique, and GFP signaling derived by auxin response promoter DR5 were weaker in hda9 and hda6 hda9 than wild type and hda6. Thus, our findings reveal that HDA6 and HDA9 coordinately control silique valve cell elongation through affecting auxin signaling related genes expression in silique.
2018-12-30 | GSE122047 | GEO
Project description:Lysine acetylation is a common post-translational modification in eukaryotes and prokaryotes which is known to be involved in the regulation of various cellular processes, such as transcriptional activation, metabolic signaling, and energy homeostasis. Nevertheless, its role in plant primary metabolism, and photosynthesis in particular, is not well understood. Lysine acetylation is catalyzed by acetyltransferases (KATs) and removed by corresponding deacetylases (KDACs). The Arabidopsis thaliana genome encodes for at least 16 KATs and 18 KDACs, belonging to seven different gene families. The cellular functions of these enzymes have been explored only partially, describing effects of single enzymes and their interaction with specific targets. In this dataset we investigated the effect of two distinct lysine deacetylase inhibitors on protein lysine acetylation in Arabidopsis thaliana leaves on a proteome-wide scale. Trichostatin A (TSA), an inhibitor of class I and II KDACs, and apicidin, an inhibitor of class I KDACs, were applied in solution to leaf strips to induce KDAC inhibition. Proteins were extracted and digested using an adapted FASP procedure, peptides were dimethyl-labeled, ZIC-HILIC fractionated and lysine-acetylated peptides were antibody-enriched. Peptide identification and quantitative data analysis was carried out using MaxQuant.
2017-10-25 | PXD006695 | Pride
Project description:Previous results suggest that Bmh might inhibit the activity of the transcription factor Adr1 after binding to Adr1-dependent promoters. In a strain lacking the two major histone deacetylases, Hda1 and Rpd3 (hdac∆), Adr1 is bound to its target promoters recruiting what appears to be an inactive RNA ploymerase II preinitiation complex (PIC). To determine whether Bmh activity inhibits this inactive PIC and the generality of this effect on glucose-repressed gene expression, the mRNA profiles of wild type, bmh mutant, hdac mutant, and bmh hdac mutant cells grown in high glucose medium were compared.
2013-01-15 | GSE40116 | GEO