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Michael Reagan, Biology


The nuclease proteins involved in eukaryotic nucleotide excision repair (NER) have been identified and are ubiquitous for most eukaryotes, including XPF (3’ endonuclease) and XPG (5’ endonuclease). Proteins with similar structures have been identified in archaeal genomes and have been shown to exhibit endonuclease activity, but their overall cellular functions have not been elucidated. The proteins Hef1 and Bax1 in archaea are two of such proteins that are candidates for homology with the XPF (Rad1 in Saccharomyces cerevisiae) nuclease. By inserting plasmids containing archaeal genes coding for these possible homologous nucleases into Saccharomyces cerevisiae without Rad1 gene (ΔRad1) and then exposing the cells to Ultraviolet (UV) light, NER function can be analyzed using survival rates. These experiments aim to investigate the function of these potential homologous XPF nucleases present in archaea.

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