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Histone H1 loss drives lymphoma by disrupting 3D chromatin architecture
- Authors
- Yusufova, NevinTeater, MattCesarman, EthelMelnick, Ari M.1 more author(s)...
- Description
Summary from the GEO: "Linker histone H1 proteins bind to nucleosomes and cause chromatin compaction, although little is known about their biological functions. Histone H1 (HIST1H1B-E) mutations are highly recurrent in B-cell lymphomas and are present in solid tumors, but their cancer relevance and mechanism are unknown. Here we report that lymphoma-associated H1 alleles are genetic driver mutations...
- Subject
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B-LymphocytesGene SilencingGenes, Tumor SuppressorHistonesLymphomaSequence Analysis
- Access Rights
- Free to All
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A multivalent signal-transducing model for the DNMT1-mediated maintenance DNA methylation
- Authors
- Wang, Gang G.Grimm, Sara A.
- Description
Summary from the GEO: "Heterochromatin-specific histone modifications frequently coexist with mammalian DNA methylation to orchestrate a repressive chromatin state. However, it remains elusive how these epigenetic modifications crosstalk. Here, we report that the first bromoadjacent homology (BAH1) domain and the replication foci targeting sequence (RFTS) of maintenance DNA methyltransferase DNMT1...
- Subject
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DNA (Cytosine-5-)-Methyltransferase 1DNA MethylationHeterochromatinHistone CodeHistones
- Access Rights
- Free to All
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Crystal structure of bovine DNMT1 BAH1 domain in complex with H4K20me2
- Authors
- Ren, WendanSong, Jikui
- Description
This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes x-ray diffraction data used for modeling the crystal structure of bovine DNMT1 BAH1 domain in complex with H4K20me2. The main summary display for this entry includes information on the experimental data, validation, macromolecules, small molecules, version history and funding identification. Data...
- Subject
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DNA (Cytosine-5-)-Methyltransferase 1HistonesMethyltransferasesRepressor Proteins
- Access Rights
- Free to All
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Crystal structure of bovine DNMT1 BAH1 domain in complex with H4K20me3
- Authors
- Ren, WendanSong, Jikui
- Description
This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes x-ray diffraction data used for modeling the crystal structure of bovine DNMT1 BAH1 domain in complex with H4K20me3. The main summary display for this entry includes information on the experimental data, validation, macromolecules, small molecules, version history and funding identification. Data...
- Subject
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DNA (Cytosine-5-)-Methyltransferase 1HistonesMethyltransferasesRepressor Proteins
- Access Rights
- Free to All
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Histone H3 threonine 11 phosphorylation is catalyzed directly by the meiosis-specific kinase Mek1 and provides a molecular readout of Mek1 activity in vivo
- Authors
- Kniewel, RyanMurakami, HajimeLiu, YanIto, Masaru3 more author(s)...
- Description
Summary from the GEO: "Saccharomyces cerevisiae Mek1 is a CHK2/Rad53-family kinase that regulates meiotic recombination and progression upon its activation in response to DNA double-strand breaks (DSBs). The full catalog of direct Mek1 phosphorylation targets remains unknown. Here, we show that phosphorylation of histone H3 on threonine 11 (H3 T11ph) is induced by meiotic DSBs in S. cerevisiae and...
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Checkpoint Kinase 2Chromatin Immunoprecipitation SequencingHistonesPhosphorylationProtein-Serine-Threonine Kinases
- Access Rights
- Free to All
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Whole genome ChIP-seq of histone H3 threonine 11 phosphorylation in Saccharomyces cerevisiae
- Authors
- Murakami, HajimeKniewel, RyanKeeney, Scott
- Description
Summary from the GEO: "We used ChIP-seq to determine the whole-genome enrichment of histone H3 threonine 11 phosphorylation (H3 T11ph) during Saccharomyces cerevisiae meiosis. S. cerevisiae SK1 cells were synchronized for meiotic entry and 3 and 4 hour meiotic samples were obtained. As H3 T11ph is dependent on the formation of meiotic double strand breaks (DSBs), a negative control ChIP-seq sample...
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Chromatin Immunoprecipitation SequencingHistonesPhosphorylationProtein-Serine-Threonine Kinases
- Access Rights
- Free to All
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Proteomics Data for "DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network"
- Authors
- Hendriks, IvoNielsen, Michael L.
- Description
Description from PRIDE: "From biosynthesis to assembly into nucleosomes, histones are handed through a cascade of histone chaperones, which shield histones from non-specific interactions. Whether mechanisms exist to safeguard the histone fold during histone chaperone handover events or to release trapped intermediates is unclear. Using structure-guided and functional proteomics, we identify and characterize...
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Histone ChaperonesHistonesHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMinichromosome Maintenance Complex Component 2
- Access Rights
- Free to All
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DNAJC9 Integrates Heat Shock Molecular Chaperones into the Histone Chaperone Network
- Authors
- Hammond, Colin M.Reverón-Gómez, NazaretGroth, Anja
- Description
Summary from the GEO: "From biosynthesis to assembly into nucleosomes, histones are handed through a cascade of histone chaperones, which shield histones from non-specific interactions. Whether mechanisms exist to safeguard the histone fold during histone chaperone handover events or to release trapped intermediates is unclear. Using structure-guided and functional proteomics, we identify and characterize...
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Histone ChaperonesHistonesHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMinichromosome Maintenance Complex Component 2
- Access Rights
- Free to All
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Crystal structure of DNAJC9 HBD helix2 in complex with H3.3-H4 dimer and MCM2 HBD
- Authors
- Bao, HongyuHuang, Hongda
- Description
This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes electron microscopy data identifying the crystal structure of DNAJC9 HBD helix2 in complex with H3.3-H4 dimer and MCM2 HBD. The main summary display for this entry includes information on the experimental method, validation, macromolecules and small molecules included in the deposit, as well as...
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Histone ChaperonesHistonesHSP40 Heat-Shock ProteinsMinichromosome Maintenance Complex Component 2
- Access Rights
- Free to All
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Crystal structure of DNAJC9 HBD in complex with H3.3-H4 dimer and MCM2 HBD
- Authors
- Bao, HongyuHuang, Hongda
- Description
This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes electron microscopy data identifying the crystal structure of DNAJC9 HBD in complex with H3.3-H4 dimer and MCM2 HBD. The main summary display for this entry includes information on the experimental method, validation, macromolecules and small molecules included in the deposit, as well as version...
- Subject
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Histone ChaperonesHistonesHSP40 Heat-Shock ProteinsMinichromosome Maintenance Complex Component 2
- Access Rights
- Free to All