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Expression data from wild-type and H2B K37A mutant yeast histones

ABSTRACT: We identified lysine 37 of histone H2B as a novel site of histone lysine methylation in budding yeast. Microarray analysis was performed to determine global changes in gene expression upon mutation of this lysine residue to a unmodifiable form.

ORGANISM(S): Saccharomyces cerevisiae Schizosaccharomyces pombe

PROVIDER: GSE24380 | GEO | 2010/09/27

SECONDARY ACCESSION(S): PRJNA132865

REPOSITORIES: GEO

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Expression data from wild-type and H2B K37A mutant yeast histones

Project description:We identified lysine 37 of histone H2B as a novel site of histone lysine methylation in budding yeast. Microarray analysis was performed to determine global changes in gene expression upon mutation of this lysine residue to a unmodifiable form. Histones were acid-extracted from asynchronously grown yeast expressing wild-type H2B or H2B harboring a K37A mutation.

2010-09-26 | E-GEOD-24380 | biostudies-arrayexpress

Histone H2B^3-32, H2B K->G, H2B^3-37, and H2B^30-37 mutations

Project description:Histone H2B^3-32, H2B K->G, H2B^3-37, and H2B^30-37 mutations

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Histone H2B^3-32, H2B K->G, H2B^3-37, and H2B^30-37 mutations

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Histone H2B^30-37

Project description:Histone H2B was mutated to give H2B^30-37. Total RNA from three replicate cultures of wild-type and mutant was isolated and the expression profiles were determined using Affymetrix arrays. Comparisons between the sample groups allow the identification of genes regulated by H2B HBR domain. Keywords: repeat

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Histone H2B^3-37

Project description:Histone H2B was mutated to give H2B^3-37. Total RNA from three replicate cultures of wild-type and mutant was isolated and the expression profiles were determined using Affymetrix arrays. Comparisons between the sample groups allow the identification of genes regulated by H2B N-terminal domain. Keywords: repeat

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Transcription profiling of S. cerevisiae wild type and amino-terminus mutant histone H2B (HTB1) strains

Project description:Histone H2B was mutated to give H2B^3-32, H2B K->G, H2B^3-37, and H2B^30-37. Total RNA from three replicate cultures of wild-type and mutant was isolated and the expression profiles were determined using Affymetrix arrays. Comparisons between the sample groups allow the identification of genes regulated by H2B HBR domain. Experiment Overall Design: mutants compared to wild-type, 3 replicates Experiment Overall Design: This reference Series links data in the following related Series: Experiment Overall Design: GSE3802 Histone H2B^3-32 Experiment Overall Design: GSE3803 Histone H2B K->G Experiment Overall Design: GSE3804 Histone H2B^3-37 Experiment Overall Design: GSE3805 Histone H2B^3-37

2007-09-21 | E-GEOD-3806 | biostudies-arrayexpress

methylation sites of Histone H2B catalyzed by LaeA

Project description:In Penicillium oxalicum, histone H2B (PDE_01489) was one of the interacting proteins with the methyltransferase LaeA. It suggests that histone H2B may be a direct target of LaeA/Lae1. To verify whether histone H2B is one of the LaeA targets, an in vitro catalytic experiment was performed using Homo sapiens recombinant histone H2B (HsH2B, expressed in Escherichia coli, without histone modification), SAM as substrates, and LaeA. The products were analyzed by LC-MS/MS for histone modifications. Results showed that the mono and di-methylation of lysine 108 and the mono-methylation of lysine 116 were detected.

2021-07-08 | PXD027171 | iProX

Molecular basis of RanGTP-activated release of Histones H2A-H2B from Importin-9

Project description:Imp9 is the primary importin for shuttling H2A-H2B from the cytoplasm to the nucleus. It employs an unusual mechanism where the binding of RanGTP is insufficient to release H2A-H2B. The resulting stable RanGTP•Imp9•H2A-H2B complex gains nucleosome assembly activity with H2A-H2B able to be deposited into an assembling nucleosome in vitro. Using hydrogen-deuterium exchange coupled with mass spectrometry (HDX), we show that Imp9 stabilizes H2A-H2B beyond the direct binding site, like other histone chaperones. HDX also shows that binding of RanGTP releases H2A-H2B contacts at Imp9 HEAT repeats 4-5, but not 18-19. DNA- and histone-binding surfaces of H2A-H2B are exposed in the ternary complex, facilitating nucleosome assembly. We also reveal that RanGTP has a weaker affinity for Imp9 when H2A-H2B is bound. Imp9 thus provides a connection between the nuclear import of H2A-H2B and its deposition into chromatin.

2023-06-02 | PXD037571 | Pride

GlcNAcylation of histone H2B facilitates its monoubiquitination [Affymetrix data]

Project description:We have found that histone H2B is GlcNAcylated at residue S112 by O-GlcNAc transferase and that H2B S112 GlcNAcylation fluctuates in response to extracellular glucose level. We have also found that H2B S112 GlcAcylation promotes H2B K120 ubiquitination. To investigate whether these histone modification correlate to transcriptional activation, we performed comprehensive gene expression analysis using Affymetrix GeneChip in HeLa cell cultured with different conditions, i.e. without glucose, with glucose and with FBS.

2011-10-27 | GSE33050 | GEO

A Basic Domain in the Histone H2B N-terminal Tail is Important for Nucleosome Assembly by FACT

Project description:Nucleosome assembly in vivo requires assembly factors, such as histone chaperones, to bind to histones and mediate their deposition onto DNA. In yeast, the essential histone chaperone FACT (FAcilitates Chromatin Transcription) functions in nucleosome assembly and H2A-H2B deposition during transcription elongation and DNA replication. Recent studies have identified candidate histone residues that mediate FACT binding to histones, but it is not known which histone residues are important for FACT to deposit histones onto DNA during nucleosome assembly. In this study, we report that the histone H2B repression (HBR) domain within the H2B N-terminal tail is important for histone deposition by FACT. Deletion of the HBR domain causes significant defects in histone occupancy in the yeast genome, particularly at HBR-repressed genes, and a pronounced increase in H2A-H2B dimers that remain bound to FACT in vivo. Moreover, the HBR domain is required for purified FACT to efficiently assemble recombinant nucleosomes in vitro. We propose that the interaction between the highly basic HBR domain and DNA plays an important role in stabilizing the nascent nucleosome during the process of histone H2A-H2B deposition by FACT. 6 samples, 2 inputs and 4 ChIP samples for histone H2B (2 for wild-type and 2 for an H2B â30-37 mutant)

2016-08-10 | E-GEOD-80831 | biostudies-arrayexpress

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