Arabidopsis thaliana
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA360334 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR5149631.fastq.gz | Fastqsanger.gz | |||
| SRR5149632.fastq.gz | Fastqsanger.gz | |||
| SRR5149633.fastq.gz | Fastqsanger.gz | |||
| SRR5149634.fastq.gz | Fastqsanger.gz | |||
| SRR5149635.fastq.gz | Fastqsanger.gz |
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Project description:Histone variants are critical determinants for chromatin function with diverse regulatory mechanisms. The H3 variants, H3.1 and H3.3, evolved independently in animals and plants. A significant difference between H3.1 and H3.3 is the amino acid variation at position 31, with H3.1 carrying alanine (A), while H3.3 bearing serine (S) in animals or threonine (T) in plants. Both S and T can be phosphorylated, but why plants have selectively adopted T over S remains unclear. Here, we report the specific role of plant H3.3T31 in controlling plant development and stress responses by promoting the deposition of histone H3 lysine 36 trimethylation (H3K36me3) on H3.3. T31 prevents plant-specific H3K27 methyltransferases, ATXR5 and ATXR6, from depositing H3K27 monomethylation (H3K27me1), which inhibits the activity of H3K36 methyltransferase EFS. Substituting H3.3T31 with an S or A residue results in increased ATXR5/6 activity and elevated H3K27me1 levels, leading to a reduction in H3K36me3. Moreover, we show that unlike H3.3 T31S and T31A mutations, cancer-associated G34R and G34W mutations directly disrupt H3K36me3 deposition without affecting H3K27me1. These G34 mutations may also influence H3.3 function through mechanisms beyond the disruption of H3K36me3. Our data suggest a co-evolution of the plant-specific H3.3T31 residue and H3K27 methyltransferases ATXR5/6, which ensures the selective accumulation of H3K27me1 on H3.1 and H3K36me3 on H3.3, thereby enabling proper chromatin function.
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Project description:Nucleosomes package eukaryotic DNA and are composed of four different histone proteins, H3, H4, H2A and H2B. Histone H3 has two main variants, H3.1 and H3.3, which show different genomic localization patterns in animals. We profiled H3.1 and H3.3 variants in the genome of the plant Arabidopsis thaliana and show that the localization of these variants shows broad similarity in plants and animals, in addition to some unique features. H3.1 was enriched in silent areas of the genome including regions containing the repressive chromatin modifications H3 lysine 27 methylation, H3 lysine 9 methylation, and DNA methylation. In contrast, H3.3 was enriched in actively transcribed genes, especially peaking at the 3’ end of genes, and correlated with histone modifications associated with gene activation such as histone H3 lysine 4 methylation, and H2B ubiquitylation, as well as by RNA Pol II occupancy. Surprisingly, both H3.1 and H3.3 were enriched on defined origins of replication, as was overall nucleosome density, suggesting a novel characteristic of plant origins. Our results are broadly consistent with the hypothesis that H3.1 acts as the canonical histone that is incorporated during DNA replication, whereas H3.3 acts as the replacement histone that can be incorporated outside of S-phase during chromatin disrupting processes like transcription.
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