FACULTY & STAFF DIRECTORY
|
PhD Student
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| Group |
Kobor Lab |
| Email |
 |
| Direct line |
+1 (604) 875-3833 |
| Fax |
+1 (604) 875-3840 |
|
ADDITIONAL CONTACT INFORMATION
| Location |
Room 2003 |
|
Centre for Molecular Medicine and Therapeutics 950 West 28th Avenue Vancouver, BC V5Z 4H4 Canada |
TRAINEE INFORMATION
| Degree sought |
PhD |
| Thesis topic |
Functional Roles of the BRCT-Domain protein Rtt107 in the DNA Damage Response |
| Grad advisor |
Dr. Michael S. Kobor |
RESEARCH INTERESTS
Maintenance of genome integrity is critical for proper cellular function, with perturbations potentially having serious ramifications for health and disease, as best exemplified by cancer development. It is therefore vital to characterize the molecular mechanisms that stabilize the genome, including pathways for repair of DNA damaged through constant assault by chemicals or processes such as stalling of DNA replication forks. A common hallmark of the DNA damage response is the assembly of large protein complexes, often orchestrated in a distinct temporal and spatial sequence. This is mediated by specialized scaffolding proteins, which frequently share BRCT (BRCA1 C-terminal) domains as a key structural feature. Importantly, the mechanisms for DNA damage response appear to be conserved throughout evolution, providing the opportunity to take advantage of simple organisms such as yeast to allow for detailed genetic, biochemical and mechanistic investigations. My research focuses on the function of yeast Rtt107, a nuclear protein containing six BRCT domains which is important for the cellular response to DNA damage during S-phase. However, the genetic mechanisms, regulatory pathways, and protein complexes converging on Rtt107 remain to be fully discovered and are the central focus of my thesis project.
AWARDS & HONORS
NSERC Alexander Graham Bell Canada Graduate Scholarship
Publications
Journal Articles
1 Leung GP, Lee L, Schmidt TI, Shirahige K, Kobor MS.
Rtt107 is required for recruitment of the SMC5/6 complex to DNA double strand breaks. J. Biol. Chem. 286(29):26250-7. (2011)
PMID 21642432 2 Lévesque N, Leung GP, Fok AK, Schmidt TI, Kobor MS.
Loss of H3 K79 trimethylation leads to suppression of Rtt107-dependent DNA damage sensitivity through the translesion synthesis pathway. J. Biol. Chem. 285(45):35113-22. (2010)
PMID 20810656