DVE-1 is a telomere-binding protein and links the NuRD complex to telomere regulation in C. elegans
TL;DR
DVE-1 immunoprecipitation followed by mass spectrometry revealed all the core components of the nucleosome remodeling and deacetylase (NuRD) complex as interaction partners, implicating DVE-1 in the coordination of NuRD complex activity in the context of telomere organization.
Abstract
Summary Telomeres are repetitive DNA sequences at the ends of linear chromosomes bound by specialized proteins. In our previous quantitative proteomics screen for telomere-binding proteins of Caenorhabditis elegans, we identified DVE-1, a homolog of mammalian SATB proteins and a transcription factor, as a telomere repeat-binding protein. Here, we validate DVE-1 as a telomere-binding protein in C. elegans, demonstrating in vitro binding of DVE-1 to the single-stranded C-rich telomeric sequence and in vivo co-localization with the telomere-binding protein POT-1. RNA interference-mediated knockdown of dve-1 resulted in reduced TERRA expression and enhanced compaction of telomeric chromatin. Subsequent transcriptomic and proteomic analyses suggest a role for DVE-1 in the regulation of telomeric chromatin organization. Finally, DVE-1 immunoprecipitation followed by mass spectrometry revealed all the core components of the nucleosome remodeling and deacetylase (NuRD) complex as interaction partners, implicating DVE-1 in the coordination of NuRD complex activity in the context of telomere organization.