Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR20139900_1.fastq.gz | Fastqsanger.gz | |||
| SRR20139900_2.fastq.gz | Fastqsanger.gz | |||
| SRR20139901_1.fastq.gz | Fastqsanger.gz | |||
| SRR20139901_2.fastq.gz | Fastqsanger.gz | |||
| SRR20139902_1.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.
2026-01-29 | GSE290160 | GEO
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: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: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:The protein modules known as SH2 (Src-homology-2) domains are key players in the signal transduction of animals. Two questions arise: Do such modules exist in plants, and when did SH2 domains evolve? Here I show that the Arabidopsis genome contains three strong candidates for plant SH2 proteins (referred to as PASTA1, 2 and 3 : GI:25513455, At1g78540, At1g17040 respectively) with homology to the SH2 domains and the adjacent linker region of STAT proteins (Signal Transducer and Activator of Transcription). The three characteristics features of a STAT protein sequence1, namely, (i) the SH2 domain with a conserved arginine residue crucial for binding to a phospho-tyrosine residue (ii) a tyrosine residue outside the C-terminus of the SH2-domain for phosphorylation during signalling and (iii) a DNA-binding domain, are conserved in the PASTA3 protein. However, PASTA 1 and 2 proteins lack a tyrosine in a similar position. PASTA proteins are not homologous to STAT proteins outside the SH2 and linker regions. The three PASTA proteins are 70 to 80 % identical to one another. Gene expression studies with PASTA2 reveal that it is expressed in roots, stem, leaves, flowers and green siliques. Preliminary indications are that plants homozygous for PASTA2 do not have any obvious phenotype, most likely due to redundancies. This microarray experiment is an attempt to compare the gene expression of a mutant plant homozygous for PASTA2 with that of the wild type plant. This might give clues about the possible function of PASTA2 in Arabidopsis.
2008-02-15 | E-NASC-68 | biostudies-arrayexpress
Project description:Plant-specific histone residue F41 restricts H3.1 distribution in heterochromatin
| PRJNA360334 | ENA
Project description:The protein modules known as SH2 (Src-homology-2) domains are key players in the signal transduction of animals. Two questions arise: Do such modules exist in plants, and when did SH2 domains evolve? Here I show that the Arabidopsis genome contains three strong candidates for plant SH2 proteins (referred to as PASTA1, 2 and 3 : GI:25513455, At1g78540, At1g17040 respectively) with homology to the SH2 domains and the adjacent linker region of STAT proteins (Signal Transducer and Activator of Transcription). The three characteristics features of a STAT protein sequence1, namely, (i) the SH2 domain with a conserved arginine residue crucial for binding to a phospho-tyrosine residue (ii) a tyrosine residue outside the C-terminus of the SH2-domain for phosphorylation during signalling and (iii) a DNA-binding domain, are conserved in the PASTA3 protein. However, PASTA 1 and 2 proteins lack a tyrosine in a similar position. PASTA proteins are not homologous to STAT proteins outside the SH2 and linker regions. The three PASTA proteins are 70 to 80 % identical to one another. Gene expression studies with PASTA2 reveal that it is expressed in roots, stem, leaves, flowers and green siliques. Preliminary indications are that plants homozygous for PASTA2 do not have any obvious phenotype, most likely due to redundancies. This microarray experiment is an attempt to compare the gene expression of a mutant plant homozygous for PASTA2 with that of the wild type plant. This might give clues about the possible function of PASTA2 in Arabidopsis. Experimenter name = Latha Kadalayil; Experimenter phone = 023-8059 5512; Experimenter department = University of Southampton; Experimenter address = School of Biological Sciences; Experimenter address = Univ. Southampton; Experimenter address = Bassett Crescent East; Experimenter address = Southampton; Experimenter zip/postal_code = SO16 7PX; Experimenter country = UK Experiment Overall Design: 2 samples were used in this experiment
2008-06-13 | E-GEOD-5619 | biostudies-arrayexpress
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.
2026-01-29 | GSE290278 | GEO
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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