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Methylation of histone H3 lysine-79 by Dot1p plays multiple roles in the response to UV damage in Saccharomyces cerevisiae.

DNA repair | Mar 1, 2007

http://www.ncbi.nlm.nih.gov/pubmed/17267293

Various proteins have been found to play roles in both the repair of UV damaged DNA and heterochromatin-mediated silencing in the yeast Saccharomyces cerevisiae. In particular, factors that are involved in the methylation of lysine-79 of histone H3 by Dot1p have been implicated in both processes, suggesting a bipartite function for this modification. We find that a dot1 null mutation and a histone H3 point mutation at lysine-79 cause increased sensitivity to UV radiation, suggesting that lysine-79 methylation is important for efficient repair of UV damage. Epistasis analysis between dot1 and various UV repair genes indicates that lysine-79 methylation plays overlapping roles within the nucleotide excision, post-replication and recombination repair pathways, as well as RAD9-mediated checkpoint function. In contrast, epistasis analysis with the H3 lysine-79 point mutation indicates that the lysine-to-glutamic acid substitution exerts specific effects within the nucleotide excision repair and post-replication repair pathways, suggesting that this allele only disrupts a subset of the functions of lysine-79 methylation. The overall results indicate the existence of distinct and separable roles of histone H3 lysine-79 methylation in the response to UV damage, potentially serving to coordinate the various repair processes.

Pubmed ID: 17267293 RIS Download

Mesh terms: Adenosine Triphosphatases | Cell Cycle Proteins | DNA | DNA Damage | DNA Helicases | DNA Repair | DNA Replication | Dose-Response Relationship, Radiation | Histone-Lysine N-Methyltransferase | Histones | Lysine | Methylation | Nuclear Proteins | Radiation, Ionizing | Recombination, Genetic | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Ultraviolet Rays

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