Chemical modifications of histones play an important role in regulating access to DNA. One such modification, acetylation, has been found to be important in regulating a number of biological responses, not least of which is DNA damage repair. However, there is still a large gap in our understanding of how histone acetylation and DNA damage repair coordinate with each other to facilitate DNA access and repair. This gap in knowledge limits our understanding of the targetability of this process for therapeutic purposes. Our work utilizes mass spectrometry analysis to quickly and efficiently map chemical changes on histones. This analysis is coupled with a <i>Drosophila</i> model system, which allows us to observe biological changes in histone acetylation in response to DNA damage. We have begun identifying sites of histone acetylation that are important to the DNA damage response, as well as the timing of this dynamic process. Ultimately, our goal is to use the information gained from these investigations to identify key markers of the histone acetylation response to DNA damage.  This would allow for the potential to impair the DNA damage repair response as a novel avenue to augment the efficacy of cancer therapies that rely on DNA damage as their mechanism of action.

Mass spectrometry analysis to study histone acetylation changes in <i>Drosophila</i>

ACS Fall 2021

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Mass spectrometry analysis to study histone acetylation changes in Drosophila