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Metabolomics,Unknown,Transcriptomics,Genomics,Proteomics

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Gene expression changes in a histone sprocket arginine mutant in histone H2A R78A

ABSTRACT: Examined gene expression changes in a histone H2A R78A mutant in Saccharomyces cerevisiae relative to wild-type cells. THe overall goal of this study was to determine the functions of histone 'sprocket' arginine residues, which insert into the DNA minor groove in the nucleosome. We examined the roles of sprocket arginine mutants in gene expression, histone incorporation, and DNA repair. Three wild-type control replicate samples and three experimental (H2A R78A) replicates

ORGANISM(S): Saccharomyces cerevisiae

SUBMITTER: John Wyrick

PROVIDER: E-GEOD-68159 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Histone Sprocket Arginine Residues Are Important for Gene Expression, DNA Repair, and Cell Viability in Saccharomyces cerevisiae.

Hodges Amelia J AJ Gallegos Isaura J IJ Laughery Marian F MF Meas Rithy R Tran Linh L Wyrick John J JJ

Genetics 20150512 3

A critical feature of the intermolecular contacts that bind DNA to the histone octamer is the series of histone arginine residues that insert into the DNA minor groove at each superhelical location where the minor groove faces the histone octamer. One of these "sprocket" arginine residues, histone H4 R45, significantly affects chromatin structure in vivo and is lethal when mutated to alanine or cysteine in Saccharomyces cerevisiae (budding yeast). However, the roles of the remaining sprocket arg ...[more]

PMID: 25971662

Similar Datasets

Gene expression changes in a histone sprocket arginine mutant in histone H2A R78A

Project description:Examined gene expression changes in a histone H2A R78A mutant in Saccharomyces cerevisiae relative to wild-type cells. THe overall goal of this study was to determine the functions of histone 'sprocket' arginine residues, which insert into the DNA minor groove in the nucleosome. We examined the roles of sprocket arginine mutants in gene expression, histone incorporation, and DNA repair.

2015-08-05 | GSE68159 | GEO

Expression data from Saccharomyces cerevisiae histone H2A mutants

Project description:The N-terminal tail of histone H2A shows evolutionary changes that parallel genome size and aid chromatin compaction. As genome size increases, so does the number of arginines. In contrast, serines corellate with small genomes. Examples for such changes are arginine in position 11 and serine in position 15. To test if these residues affect mRNA levels, we analysed gene expression profiles of S.cerevisiae strains containing either WT or mutant H2A. Yeast strains have endogenous histone H2A genes deleted and express plasmid born WT or mutant H2A. PolyA RNA of these strains was analyzed by single channel microarray hybridization. Three WT biological replicates provide the control. Two biological replicates of each of the mutants containing either R11, K11, carrying a deletion in S15 and the double mutant carrying both the deletion of S15 and an insertion of R11 are analysed.

2014-03-01 | E-GEOD-50440 | biostudies-arrayexpress

Expression data from Saccharomyces cerevisiae histone H2A mutants

2014-03-01 | GSE50440 | GEO

Histone H2A K4,7G

Project description:Total RNA from three replicate cultures of wild-type and mutant strains was isolated and the expression profiles were determined using Affymetrix arrays. Comparisons between the sample groups allow the identification of genes regulated by the histone H2A K4,7G mutant. Keywords: histone H2A mutant, repeat

2007-10-11 | GSE7338 | GEO

Histone H2A^4-20

Project description:Total RNA from three replicate cultures of wild-type and mutant strains was isolated and the expression profiles were determined using Affymetrix arrays. Comparisons between the sample groups allow the identification of genes regulated by histone H2A^4-20 mutant. Keywords: histone H2A mutant, repeat

2007-10-11 | GSE7337 | GEO

Glutamine methylation on Histone H2A is an RNA Polymerase I dedicated modification

Project description:Nucleosomes are decorated with numerous post-translational modifications capable of influencing many DNA processes. Here, we describe a new class of modification, methylation of glutamine, occurring on yeast histone H2A at position 105 (Q105) and human H2A at Q104. We identify Nop1 as the methyltransferase in yeast and we demonstrate that Fibrillarin is the equivalent enzyme in human cells. Glutamine methylation of H2A is restricted to the nucleolus. Global analysis in yeast, using a H2AQ105me specific antibody, show that this modification is exclusively enriched over the 35S rDNA transcriptional unit. We show that the Q105 residue is part of the binding site for the histone chaperone FACT (Facilitator of Transcription) complex. Methylation of Q105 or its substitution to alanine disrupts binding to FACT in vitro. A yeast strain mutated at Q105 exhibits a defect in histone incorporation and shows increased transcription at rDNA genes. This defect is phenocopied by mutations in FACT that decrease its activity. Together these data identify glutamine methylation of H2A as the first histone epigenetic mark dedicated to a specific RNA polymerase and define its function as a regulator of FACT interaction with nucleosomes.

2014-01-21 | E-MTAB-1447 | biostudies-arrayexpress

Histone arginine demethylation by RDMe1

Project description:Histone arginine demethylation by RDMe1

| PRJNA514095 | ENA

dKDM2 couples histone H2A ubiquitylation to histone H3 demethylation during Polycomb group silencing.

Project description:Transcription regulation involves enzyme-mediated changes in chromatin structure. Here, we describe a novel mode of histone crosstalk during gene silencing, in which histone H2A monoubiquitylation is coupled to the removal of histone H3 Lys 36 dimethylation (H3K36me2). This pathway was uncovered through the identification of dRING-associated factors (dRAF), a novel Polycomb group (PcG) silencing complex harboring the histone H2A ubiquitin ligase dRING, PSC and the F-box protein, and demethylase dKDM2. In vivo, dKDM2 shares many transcriptional targets with Polycomb and counteracts the histone methyltransferases TRX and ASH1. Importantly, cellular depletion and in vitro reconstitution assays revealed that dKDM2 not only mediates H3K36me2 demethylation but is also required for efficient H2A ubiquitylation by dRING/PSC. Thus, dRAF removes an active mark from histone H3 and adds a repressive one to H2A. These findings reveal coordinate trans-histone regulation by a PcG complex to mediate gene repression. Microarray analysis of dKDM2, dRING, PC, PH and PSC target genes in Drosophila S2 cells Expression profiles of Drosophila S2 cells RNAi depleted (KD) for dKDM2, dRING, PC, PH or PSC were compared with expression profile of untreated S2 cells (Mock)

2011-12-13 | E-GEOD-34390 | biostudies-arrayexpress

Ubiquitinated histone H2A mapping in Drosophila ML-DmBG3 cells

Project description:Monoubiquitinated histone H2A produced by the Sce/Ring subunit of the Polycomb Repressive Complex 1 (PRC1) was mapped genome-wide in Drosophila ML-DmBG3 cells using chromatin immunoprecipitation followed by hybridization to Affymetrix tiling arrays. ML-DmBG3 chromatin immunoprecipitated with anti-histone H2AK119ub antibody and matching input chromatin were amplified, labeled and hybridized to Affymetrix tiling arrays to determine the locations of ubiquitinated H2A genome-wide.

2013-08-09 | E-GEOD-49634 | biostudies-arrayexpress

Histone arginine demethylation by RDMe1

Project description:Histone methylation mainly occurs on lysine and arginine residues. While lysine methylation can be removed by LSD1 and JmjC domain-containing demethylases, the existence of histone arginine demethylases is highly controversial. Here, we performed a high-content cell-based screening of a cDNA library containing 2,500 nuclear proteins and identified RDMe1 as a histone arginine demethylase. Overexpression of RDMe1 in HEK293T cells reduces H3R2me1/2a and H4R3me1/2a levels. In vitro, RDMe1 specifically demethylates H3R2me1/2a and H4R3me1/2a, and generates formaldehyde and succinate. The enzymatic activity requires Fe(II) and α-ketoglutarate as cofactors. RDMe1 is mainly located in the nucleolar and regulates rRNA transcription by demethylating H3R2me2a. ChIP-seq reveals that RDMe1 demethylates H4R3me2a in the promoter in a genome-wide scale. NMR reveals that RDMe1 binds iron and substrate peptides with N and C termini, respectively. Mutation of the iron binding residues abolished the binding and the demethylase activity. Thus, we identify a histone arginine demethylase and reveal the reversibility of arginine methylation.

2022-01-09 | GSE124890 | GEO

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