Authors

Andrea J. Sitton '14, Gettysburg College

Steven W. James, Gettysburg College

Document Type

Student Research Paper

Date of Creation

Fall 2013

Department

Biology

Abstract

Bre1 is a homotetrameric E3 ubiquitin-protein ligase that heterodimerizes with Rad6, an E2 ubiquitin-conjugating enzyme, in order to ubiquitinate lysine 123 in Aspergillus nidulans. This post-translational modification promotes methylation of lysines 4 and 79 on histone H3, which are required for certain damage repair pathways and for both optimal mitotic cell growth and meiosis [1-3, 12]. ΔBre1 mutants were generated by exposing protoplasts from strains auxotrophic for pyridoxine to a three-way fusion construct made from the Bre1 5’ and 3’ flanking regions and the Aspergillus fumigatus pyroA gene, which served as a selectable marker. Molecular diagnosis was confirmed via trans-locus PCR. Phenotypic analysis indicates that the loss of Bre1 increases sensitivity to DNA damage agents, decreases mitotic cell growth, and inhibits meiosis. The severe developmental defects of ΔBre1 mutants are consistent with the known roles of Bre1 as an upstream regulator of several important cellular functions. [excerpt]

Comments

Winner of the 2014 Stock Writing Prize for Sciences

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Biology Commons

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