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Updated: Sep 11, 2026

Targeted in Situ Mutagenesis of Histone Genes in Budding Yeast
Published on: January 26, 2017
A histone H2A docking domain mutant interferes with proper yFACT-gene interactions in Saccharomyces cerevisiae
Lauren Joseph1, Sydney A Ozersky1, McKenzie G Tucker1
1Biology Department, Hendrix College, Conway, AR, United States.
Abstract:
Alterations within the nucleosomal Influences Spt16-Gene Interactions (ISGI) region, which is located on the side of the nucleosome and is comprised of histone H3 and H4 residues, shift yFACT occupancy toward the 3' ends of genes, likely due to defective yFACT dissociation following transcription. Here, we show that a single amino acid substitution within the histone H2A docking domain, H2A-I103A, similarly alters yFACT-gene interactions. These results demonstrate that histone H2A integrity is required for proper yFACT-gene interactions in vivo and suggest that the H2A docking domain promotes yFACT dissociation from genes.
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