The histone deacetylase Rpd3 regulates the heterochromatin structure ofDrosophilatelomeres

Author:

Burgio Giosalba12,Cipressa Francesca3,Ingrassia Antonia Maria Rita12,Cenci Giovanni3,Corona Davide F. V.12

Affiliation:

1. Istituto Telethon Dulbecco, c/o STEMBIO, Viale delle Scienze, Edificio 16, 90128 Palermo, Italy

2. Università degli Studi di Palermo–Dipartimento di Scienze e Tecnologie Molecolari e Biomolecolari – Sezione di Biologia Cellulare, Viale delle Scienze, Edificio 16, 90128 Palermo, Italy

3. Dipartimento di Biologia di Base ed Applicata, Università dell'Aquila, 67100 Coppito, L'Aquila, Italy

Abstract

Telomeres are specialized structures at the end of eukaryotic chromosomes that are required to preserve genome integrity, chromosome stability and nuclear architecture. Telomere maintenance and function are established epigenetically in several eukaryotes. However, the exact chromatin enzymatic modifications regulating telomere homeostasis are poorly understood. In Drosophila melanogaster, telomere length and stability are maintained through the retrotransposition of specialized telomeric sequences and by the specific loading of protecting capping proteins, respectively. Here, we show that the loss of the essential and evolutionarily conserved histone deacetylase Rpd3, the homolog of mammalian HDAC1, causes aberrant telomeric fusions on polytene chromosome ends. Remarkably, these telomere fusion defects are associated with a marked decrease of histone H4 acetylation, as well as an accumulation of heterochromatic epigenetic marks at telomeres, including histone H3K9 trimethylation and the heterochromatic protein HP2. Our work suggests that Drosophila telomere structure is epigenetically regulated by the histone deacetylase Rpd3.

Publisher

The Company of Biologists

Subject

Cell Biology

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