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

Nat Commun. 2020 Jun 4;11(1):2818. doi: 10.1038/s41467-020-16635-5.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism*
  • Animals
  • Argonaute Proteins / metabolism
  • Autoantigens / metabolism*
  • Drosophila Proteins / metabolism*
  • Drosophila melanogaster
  • Epigenesis, Genetic
  • Female
  • Gene Expression Regulation
  • Gene Silencing
  • Heterochromatin / chemistry*
  • Histone Deacetylase 1 / metabolism*
  • Histones / chemistry
  • Nucleosomes / metabolism*
  • Ovary / metabolism
  • Protein Inhibitors of Activated STAT
  • RNA, Small Interfering / metabolism*

Substances

  • Argonaute Proteins
  • Autoantigens
  • Drosophila Proteins
  • Heterochromatin
  • Histones
  • Mi-2 protein, Drosophila
  • Nucleosomes
  • Protein Inhibitors of Activated STAT
  • RNA, Small Interfering
  • Su(var)2-10 protein, Drosophila
  • HDAC1 protein, Drosophila
  • Histone Deacetylase 1
  • Adenosine Triphosphatases