Please use this identifier to cite or link to this item: https://doi.org/10.1093/nar/gky245
Title: Histone H3 lysine 36 methyltransferase mobilizes NER factors to regulate tolerance against alkylation damage in fission yeast
Authors: Lim, K.K. 
Nguyen, T.T.T. 
Li, A.Y. 
Yeo, Y.P.
Chen, E.S. 
Issue Date: 2018
Publisher: Oxford University Press
Citation: Lim, K.K., Nguyen, T.T.T., Li, A.Y., Yeo, Y.P., Chen, E.S. (2018). Histone H3 lysine 36 methyltransferase mobilizes NER factors to regulate tolerance against alkylation damage in fission yeast. Nucleic Acids Research 46 (10) : 5061-5074. ScholarBank@NUS Repository. https://doi.org/10.1093/nar/gky245
Rights: Attribution-NonCommercial 4.0 International
Abstract: The Set2 methyltransferase and its target, histone H3 lysine 36 (H3K36), affect chromatin architecture during the transcription and repair of DNA double-stranded breaks. Set2 also confers resistance against the alkylating agent, methyl methanesulfonate (MMS), through an unknown mechanism. Here, we show that Schizosaccharomyces pombe (S. pombe) exhibit MMS hypersensitivity when expressing a set2 mutant lacking the catalytic histone methyltransferase domain or a H3K36R mutant (reminiscent of a set2-null mutant). Set2 acts synergistically with base excision repair factors but epistatically with nucleotide excision repair (NER) factors, and determines the timely nuclear accumulation of the NER initiator, Rhp23, in response to MMS. Set2 facilitates Rhp23 recruitment to chromatin at the brc1 locus, presumably to repair alkylating damage and regulate the expression of brc1+ in response to MMS. Set2 also show epistasis with DNA damage checkpoint proteins; regulates the activation of Chk1, a DNA damage response effector kinase; and acts in a similar functional group as proteins involved in homologous recombination. Consistently, Set2 and H3K36 ensure the dynamicity of Rhp54 in DNA repair foci formation after MMS treatment. Overall, our results indicate a novel role for Set2/H3K36me in coordinating the recruitment of DNA repair machineries to timely manage alkylating damage. � The Author(s) 2018.
Source Title: Nucleic Acids Research
URI: https://scholarbank.nus.edu.sg/handle/10635/214042
ISSN: 0305-1048
DOI: 10.1093/nar/gky245
Rights: Attribution-NonCommercial 4.0 International
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