Roles for Histones H4 Serine 1 Phosphorylation in DNA Double Strand Break Repair and Chromatin Compaction: A Dissertation
Authors
Foley, Melissa AnneFaculty Advisor
Craig Peterson, Ph.D.Academic Program
Interdisciplinary Graduate ProgramUMass Chan Affiliations
Program in Molecular MedicineDocument Type
Doctoral DissertationPublication Date
2008-08-14Keywords
DNA RepairDNA Damage
Casein Kinase II
Histones
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Amino Acids, Peptides, and Proteins
Cells
Enzymes and Coenzymes
Fungi
Genetic Phenomena
Metadata
Show full item recordAbstract
The study of DNA templated events is not complete without considering the chromatin environment. Histone modifications help to regulate gene expression, chromatin compaction and DNA replication. Because DNA damage repair must occur within the context of chromatin, many remodeling enzymes and histone modifications work in concert to enable access to the DNA and aid in restoration of chromatin after repair is complete. CK2 has recently been identified as a histone modifying enzyme. In this study we identify CK2 as a histone H3 tail kinase in vitro, identify the phospho-acceptor site in vitro, and characterize the modification in vivo in S. cerevisiae. We also characterize the DNA damage phenotype of a strain lacking a single catalytic subunit of CK2. We further characterize the CK2- dependent phosphorylation of serine 1 of histone H4 in vivo. We find that it is recruited directly to the site of a DSB and this recruitment requires the SIN3/RPD3 histone deacetylase complex. We also characterize the contribution of H4 serine 1 phosphorylation in chromatin compaction by using reconstituted nucleosomal arrays to study folding in the analytical ultracentrifuge.DOI
10.13028/shgk-q661Permanent Link to this Item
http://hdl.handle.net/20.500.14038/31709Rights
Copyright is held by the author, with all rights reserved.ae974a485f413a2113503eed53cd6c53
10.13028/shgk-q661