Thesis
Regulation of histone H3K56 acetylation by the histone H2A-H2B acidic patch
Washington State University
Master of Science (MS), Washington State University
2012
Handle:
https://hdl.handle.net/2376/106207
Abstract
The nucleosome acidic patch is highly conserved from yeast to humans and has been shown to be an important binding interface for several protein-nucleosomal interactions. Of the four essential residues that have been identified in the H2A-H2B dimer, three (H2A Y58, E62, D91) lie within the acidic patch. Our work has demonstrated that the H2A Y58 position can accommodate the conservative tyrosine to phenylalanine mutation, while the D91 position is absolutely essential. Additionally, the H2A Y58F mutant demonstrates an increased sensitivity to HU, MMS, and UV irradiation and has a significant loss of silencing in the subtelomere region. Our results indicate that the H2A Y58F mutation induces H3K56 hyperacetylation through an ASF1 independent, Rtt109 and Vps75 dependent pathway, and that the DNA damage and Replication defects seen are not due to a disruption in the DNA damage repair pathway, but rather a disruption in the ASF1-Hir complex nucleosome deposition pathway.
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Details
- Title
- Regulation of histone H3K56 acetylation by the histone H2A-H2B acidic patch
- Creators
- Stephanie J. Kattar-Mell
- Contributors
- William B. Davis (Degree Supervisor)
- Awarding Institution
- Washington State University
- Academic Unit
- Molecular Biosciences, School of
- Theses and Dissertations
- Master of Science (MS), Washington State University
- Publisher
- Washington State University; Pullman, Wash. :
- Identifiers
- 99900525288901842
- Language
- English
- Resource Type
- Thesis