Event Title

Investigation of Functionally Important Residues in Histone Variant H2A.Z and the Effect of Rapamycin on Saccharomyces Cerevisiae

Faculty Advisor

Dr. Michael Parra

Start Date

23-4-2019 4:00 PM

End Date

23-4-2019 5:00 PM

Description

Histones are involved in the compaction of DNA and require modification to allow for normal DNA processes. One way this is done is through placement of histone variants. When wild type and yeast cells without variant H2A.Z are grown with rapamycin, a genotoxic stressor, gene expression is impacted. An rt-PCR was performed to investigate the expression of genes MEH1 and LST8, known to be involved in DNA damage response and replication. There was an increase in expression of both genes in H2A.Z yeast. We then questioned how yeast differentiate placement of H2A.Z and its canonical counterpart H2A, and the differences between them were investigated. A sequence alignment was performed and several residues unique to H2A.Z and conserved across species including T87 were identified. The expression of MEH1 and LST8 was also affected in the T87 mutants. These findings indicate that the T87 residue is important for the functionality of H2A.Z.

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Apr 23rd, 4:00 PM Apr 23rd, 5:00 PM

Investigation of Functionally Important Residues in Histone Variant H2A.Z and the Effect of Rapamycin on Saccharomyces Cerevisiae

Histones are involved in the compaction of DNA and require modification to allow for normal DNA processes. One way this is done is through placement of histone variants. When wild type and yeast cells without variant H2A.Z are grown with rapamycin, a genotoxic stressor, gene expression is impacted. An rt-PCR was performed to investigate the expression of genes MEH1 and LST8, known to be involved in DNA damage response and replication. There was an increase in expression of both genes in H2A.Z yeast. We then questioned how yeast differentiate placement of H2A.Z and its canonical counterpart H2A, and the differences between them were investigated. A sequence alignment was performed and several residues unique to H2A.Z and conserved across species including T87 were identified. The expression of MEH1 and LST8 was also affected in the T87 mutants. These findings indicate that the T87 residue is important for the functionality of H2A.Z.