The Mi-2 nucleosome remodeler and the Rpd3 histone deacetylase are involved in piRNA-guided heterochromatin formation.
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
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
04 06 2020
04 06 2020
Historique:
received:
07
11
2018
accepted:
11
05
2020
entrez:
6
6
2020
pubmed:
6
6
2020
medline:
19
8
2020
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 32499524
doi: 10.1038/s41467-020-16635-5
pii: 10.1038/s41467-020-16635-5
pmc: PMC7272611
doi:
Substances chimiques
Argonaute Proteins
0
Autoantigens
0
Drosophila Proteins
0
Heterochromatin
0
Histones
0
Mi-2 protein, Drosophila
0
Nucleosomes
0
Protein Inhibitors of Activated STAT
0
RNA, Small Interfering
0
Su(var)2-10 protein, Drosophila
0
HDAC1 protein, Drosophila
EC 3.5.1.98
Histone Deacetylase 1
EC 3.5.1.98
Adenosine Triphosphatases
EC 3.6.1.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2818Subventions
Organisme : NIH HHS
ID : P40 OD010949
Pays : United States
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