Changes in Histone H3 Acetylation on Lysine 9 Accompany Aβ 1-40 Overexpression in an Alzheimer’s Disease Yeast Model

Authors

Muna M. Hugais, CUNY Brooklyn College
Samantha N. Cobos, CUNY Graduate Center
Seth A. Bennett, CUNY Graduate Center
Jailene Paredes, CUNY Brooklyn College
Genevieve Foran, Ossining High School
Mariana P. Torrente, CUNY Brooklyn CollegeFollow

Document Type

Article

Publication Date

11-2-2021

Abstract

Alzheimer’s Disease (AD), the most common type of dementia, is a neurodegenerative disease characterized by plaques of amyloid-beta (Aβ) peptides found in the cerebral cortex of the brain. The pathological mechanism by which Aβ aggregation leads to neurodegeneration remains unknown. Interestingly, genetic mutations do not explain most AD cases suggesting that other mechanisms are at play. Epigenetic mechanisms, such as histone post-translational modifications (PTMs), may provide insight into the development of AD. Here, we exploit a yeast Aβ overexpression model to map out the histone PTM landscape associated with AD. We find a modest decrease in the acetylation levels on lysine 9 of histone H3 in the context of Aβ 1-40 overexpression. This change is accompanied by a decrease in RNA levels. Our results support a potential role for H3K9ac in AD pathology and allude to the role of epigenetics in AD and other neurodegenerative diseases.

Comments

This work was originally published in microPublication Biology, available at https://doi.org/10.17912/micropub.biology.000492

This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International (CC BY 4.0) License.