ASH1L histone methyltransferase regulates the handoff between damage recognition factors in global-genome nucleotide excision repair

Balbo Pogliano, Chiara; Gatti, Marco; Rüthemann, Peter; Garajovà, Zuzana; Penengo, Lorenza; Naegeli, Hanspeter

doi:10.1038/s41467-017-01080-8

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Balbo Pogliano, C., Gatti, M., Rüthemann, P., Garajovà, Z., Penengo, L., & Naegeli, H. (2017). ASH1L histone methyltransferase regulates the handoff between damage recognition factors in global-genome nucleotide excision repair. Nature Communications, 8(1), 1333. https://doi.org/10.1038/s41467-017-01080-8

Abstract

Global-genome nucleotide excision repair (GG-NER) prevents ultraviolet (UV) light-induced skin cancer by removing mutagenic cyclobutane pyrimidine dimers (CPDs). These lesions are formed abundantly on DNA wrapped around histone octamers in nucleosomes, but a specialized damage sensor known as DDB2 ensures that they are accessed by the XPC initiator of GG-NER activity. We report that DDB2 promotes CPD excision by recruiting the histone methyltransferase ASH1L, which methylates lysine 4 of histone H3. In turn, methylated H3 facilitates