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◆ microPublication biology2026-01-01

A histone H2A docking domain mutant interferes with proper yFACT-gene interactions in Saccharomyces cerevisiae.

Lauren Joseph, Sydney A Ozersky, McKenzie G Tucker, Grace A Turner, Michaela J Edwards, Michelle L Huynh, Andrea A Duina

原始摘要(英文原文)· Original 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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A histone H2A docking domain mutant interferes with proper yFACT-gene interactions in Saccharomyces cerevisiae. — 科研速览 Science Skim