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

Author

Listed:
  • Chiara Balbo Pogliano

    (University of Zurich-Vetsuisse)

  • Marco Gatti

    (University of Zurich
    University of Zurich)

  • Peter Rüthemann

    (University of Zurich-Vetsuisse)

  • Zuzana Garajovà

    (University of Zurich-Vetsuisse)

  • Lorenza Penengo

    (University of Zurich)

  • Hanspeter Naegeli

    (University of Zurich-Vetsuisse)

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 the docking of the XPC complex to nucleosomal histone octamers. Consequently, DDB2, ASH1L and XPC proteins co-localize transiently on histone H3-methylated nucleosomes of UV-exposed cells. In the absence of ASH1L, the chromatin binding of XPC is impaired and its ability to recruit downstream GG-NER effectors diminished. Also, ASH1L depletion suppresses CPD excision and confers UV hypersensitivity. These findings show that ASH1L configures chromatin for the effective handoff between damage recognition factors during GG-NER activity.

Suggested Citation

  • Chiara Balbo Pogliano & Marco Gatti & Peter Rüthemann & Zuzana Garajovà & Lorenza Penengo & Hanspeter Naegeli, 2017. "ASH1L histone methyltransferase regulates the handoff between damage recognition factors in global-genome nucleotide excision repair," Nature Communications, Nature, vol. 8(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-01080-8
    DOI: 10.1038/s41467-017-01080-8
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    Cited by:

    1. Corina Maritz & Reihaneh Khaleghi & Michelle N. Yancoskie & Sarah Diethelm & Sonja Brülisauer & Natalia Santos Ferreira & Yang Jiang & Shana J. Sturla & Hanspeter Naegeli, 2023. "ASH1L-MRG15 methyltransferase deposits H3K4me3 and FACT for damage verification in nucleotide excision repair," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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