Type of Submission
Poster
Keywords
Tetrahymena, mitotic regulation, H3K27, acetylation, gene regulation
Proposal
Gene regulation is one of the most complex tasks to be undertaken by any eukaryotic cell, and a prime contributor to gene regulation is the post-translational modification of histone tails. Diffuse Intrinsic Pontine Glioma (DIPG) is an example of a cancer that occurs when one lysine, H3K27 on the tail of histone H3, is mutated to a methionine, making the usual post-translational modifications (methylation and acetylation) that occur at position 27 impossible. We believe that this lysine residue is critical for the regulation of cell division. Our hypothesis was that perturbations of cell division, as well as stress, will affect acetylation at H3K27. We also sought to find some of the binding partners that interact with H3K27ac by doing whole cell CO-IP. Our results show that stress and mitotic inhibitors affect acetylation levels of H3K27, and that proteins associated with DNA repair, transcription, RNA processing, and nuclear proteostasis associate with H3K7ac.
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.
Publication Date
2024
H3K27Ac Levels are Affected by Heat Stress and Anti-Mitotic Drugs in Tetrahymena Thermophila
Gene regulation is one of the most complex tasks to be undertaken by any eukaryotic cell, and a prime contributor to gene regulation is the post-translational modification of histone tails. Diffuse Intrinsic Pontine Glioma (DIPG) is an example of a cancer that occurs when one lysine, H3K27 on the tail of histone H3, is mutated to a methionine, making the usual post-translational modifications (methylation and acetylation) that occur at position 27 impossible. We believe that this lysine residue is critical for the regulation of cell division. Our hypothesis was that perturbations of cell division, as well as stress, will affect acetylation at H3K27. We also sought to find some of the binding partners that interact with H3K27ac by doing whole cell CO-IP. Our results show that stress and mitotic inhibitors affect acetylation levels of H3K27, and that proteins associated with DNA repair, transcription, RNA processing, and nuclear proteostasis associate with H3K7ac.
