Characterization of the Dual PHD Domains of the Rco1 Protein in Rpd3S Complex Function
Public Deposited- Last Modified
- February 26, 2019
- Creator
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Neal, Jennifer Elizabeth
- Affiliation: College of Arts and Sciences, Department of Biology
- Abstract
- Chromatin, which is comprised of DNA and histone proteins, permits compaction of genetic material and variable availability of DNA for processes such as gene transcription. An improved understanding of chromatin dynamics could lead to new cancer treatments. Changes to chromatin occur in response to chemical modifications applied to and removed from histones by protein complexes. Rco1 is a protein in the Rpd3S histone deacetylase complex. The aim of this research was to determine the roles of the two PHD domains of Rco1 in Rpd3S function. I made point mutations of evolutionarily conserved bases within each domain, and studied the PHD mutants using genetic and biochemical assays. My results indicate that both PHD domains may be involved with Rpd3S function and, specifically, Rco1 binding to chromatin. This research represents the first investigation of the role of the second PHD domain, and contributes to characterization of chromatin dynamics.
- Date of publication
- spring 2014
- Keyword
- DOI
- Resource type
- Rights statement
- In Copyright
- Note
- Funding: None
- Advisor
- Strahl, Brian
- Degree
- Bachelor of Science
- Honors level
- Highest Honors
- Degree granting institution
- University of North Carolina at Chapel Hill
- Extent
- 19 pages
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