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.
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.
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. Experiment Overall Design: Comparison of genes whose mRNA levels are affected in a histone H2A^4-20 mutant yeast strain compared to wild-type yeast strain.
Project description:To study the relevance of the post-translational modification in the H2A histone residue S121, we assessed the genome-wide transcriptional response of the non-phosphorylatable histone mutant HTA1-S121A (H2AS121A) upon two different stress conditions; osmostress and heat shock. Results point out that the unphosphorylatable H2AS121A protein showed an impaired stress responsive gene expression indicating that this specific histone residue plays a relevant role in stress responsive transcriptional regulation.
