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RESEARCH INTERESTSOne of the fundamental ways that the chromatin structure can be altered is the replacement of canonical histones with non-allelic histone variants. Rather than being distributed randomly across the genome, histone variants are often found in specific locations, thus creating distinct chromosome neighborhoods. I study one such variant, H2A.Z in the budding yeast Saccharomyces cerevisiae. H2A.Z is conserved from yeast to human and replaces canonical H2A in 5-10% of nucleosomes. My research focuses on deciphering the fundamental structural and functional differences between H2A and H2A.Z using a combination of genetic, biochemical and genomic approaches. My goal is to identify regions in H2A.Z conferring functional differences from H2A.AWARDS & HONORSCanadian Institute of Health Research (CIHR) - Frederick Banting and Charles Best Canada Graduate Scholarships - Doctoral Award - 2009-2012Michael Smith Foundation for Health Research (MSFHR) - Junior Graduate Studentship - 2007-2009 PublicationsReviews and Invited Reviews1 Review Wang A. TMEM216 joins its ciliary cousins in ciliopathies. Clin. Genet. 79(1):45-7. (2011) PMID 21029074 2 Review (Invited) Schulze JM, Wang AY, Kobor MS. Reading chromatin: insights from yeast into YEATS domain structure and function. Epigenetics 5(7):573-7. (2010) PMID 20657183 3 Review (Invited) Schulze JM, Wang AY, Kobor MS. YEATS domain proteins: a diverse family with many links to chromatin modification and transcription. Biochem. Cell Biol. 87(1):65-75. (2009) PMID 19234524 Journal Articles1 Wang AY, Aristizabal MJ, Ryan C, Krogan NJ, Kobor MS. Key functional regions in the histone variant H2A.Z C-terminal docking domain. Mol. Cell. Biol. 31(18):3871-84. (2011) PMID 21791612 2 Halley JE, Kaplan T, Wang AY, Kobor MS, Rine J. Roles for H2A.Z and its acetylation in GAL1 transcription and gene induction, but not GAL1-transcriptional memory. PLoS Biol. 8(6):e1000401. (2010) PMID 20582323 3 Wang AY, Schulze JM, Skordalakes E, Gin JW, Berger JM, Rine J, Kobor MS. Asf1-like structure of the conserved Yaf9 YEATS domain and role in H2A.Z deposition and acetylation. Proc. Natl. Acad. Sci. U.S.A. 106(51):21573-8. (2009) PMID 19966225
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