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The Mi-2 nucleosome remodeler and the Rpd3 histone deacetylase are involved in piRNA-guided heterochromatin formation

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Listed:
  • Bruno Mugat

    (CNRS and Univ. Montpellier)

  • Simon Nicot

    (CNRS and Univ. Montpellier)

  • Carolina Varela-Chavez

    (CNRS and Univ. Montpellier)

  • Christophe Jourdan

    (CNRS and Univ. Montpellier)

  • Kaoru Sato

    (Graduate School of Science, The University of Tokyo)

  • Eugenia Basyuk

    (CNRS and Univ. Montpellier)

  • François Juge

    (University of Montpellier, CNRS)

  • Mikiko C. Siomi

    (Graduate School of Science, The University of Tokyo)

  • Alain Pélisson

    (CNRS and Univ. Montpellier)

  • Séverine Chambeyron

    (CNRS and Univ. Montpellier)

Abstract

In eukaryotes, trimethylation of lysine 9 on histone H3 (H3K9) is associated with transcriptional silencing of transposable elements (TEs). In drosophila ovaries, this heterochromatic repressive mark is thought to be deposited by SetDB1 on TE genomic loci after the initial recognition of nascent transcripts by PIWI-interacting RNAs (piRNAs) loaded on the Piwi protein. Here, we show that the nucleosome remodeler Mi-2, in complex with its partner MEP-1, forms a subunit that is transiently associated, in a MEP-1 C-terminus-dependent manner, with known Piwi interactors, including a recently reported SUMO ligase, Su(var)2-10. Together with the histone deacetylase Rpd3, this module is involved in the piRNA-dependent TE silencing, correlated with H3K9 deacetylation and trimethylation. Therefore, drosophila piRNA-mediated transcriptional silencing involves three epigenetic effectors, a remodeler, Mi-2, an eraser, Rpd3 and a writer, SetDB1, in addition to the Su(var)2-10 SUMO ligase.

Suggested Citation

  • Bruno Mugat & Simon Nicot & Carolina Varela-Chavez & Christophe Jourdan & Kaoru Sato & Eugenia Basyuk & François Juge & Mikiko C. Siomi & Alain Pélisson & Séverine Chambeyron, 2020. "The Mi-2 nucleosome remodeler and the Rpd3 histone deacetylase are involved in piRNA-guided heterochromatin formation," Nature Communications, Nature, vol. 11(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-16635-5
    DOI: 10.1038/s41467-020-16635-5
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