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DVE-1 is a telomere-binding protein and links the NuRD complex to telomere regulation in C. elegans

ABSTRACT: Telomeres are repetitive DNA sequences at the end of linear chromosomes bound by specialized proteins. In our previous quantitative proteomics screen for telomere-binding proteins of Caenorhabditis elegans, we identified the homeobox protein DVE-1, a homolog of mammalian SATB proteins and transcription factor that plays a central role in the mitochondrial unfolded protein response, 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 known telomere binding protein POT-1 corroborated by ChIPseq analysis. 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 identified all 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.

ORGANISM(S): Caenorhabditis elegans

PROVIDER: GSE333583 | GEO | 2026/06/23

REPOSITORIES: GEO

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Project description:Background. Telomeric small RNAs related to PIWI-interacting RNAs (piRNAs) have been described in various eukaryotes; however, their role in germline-specific telomere function remains poorly understood. Using a Drosophila model, we performed an in-depth study of the biogenesis of telomeric piRNAs and their function in telomere homeostasis in the germline. Results To fully characterize telomeric piRNA clusters, we integrated the data obtained from analysis of endogenous telomeric repeats, as well as transgenes inserted into different telomeric and subtelomeric regions. The small RNA-seq data from strains carrying telomeric transgenes demonstrated that all transgenes belong to a class of dual-strand piRNA clusters; however, their capacity to produce piRNAs varies significantly. Rhino, a paralog of heterochromatic protein 1 (HP1) expressed exclusively in the germline, is associated with all telomeric transgenes, but its enrichment correlates with the abundance of transgenic piRNAs. It is likely that this heterogeneity is determined by the sequence peculiarities of telomeric retrotransposons. In contrast to the heterochromatic non-telomeric germline piRNA clusters, piRNA loss leads to a dramatic decrease in HP1, Rhino, and trimethylated histone H3 lysine 9 in telomeric regions. Therefore, the presence of piRNAs is required for the maintenance of telomere chromatin in the germline. Moreover, piRNA loss causes telomere translocation from the nuclear periphery toward the nuclear interior but does not affect telomere end capping. Analysis of the telomere-associated sequences (TASs) chromatin revealed strong tissue specificity. In the germline, TASs are enriched with HP1 and Rhino, in contrast to somatic tissues, where they are repressed by Polycomb group proteins. Conclusions piRNAs play an essential role in the assembly of telomeric chromatin, as well as in nuclear telomere positioning in the germline. Telomeric arrays and TASs belong to a unique type of Rhino-dependent piRNA clusters with transcripts that serve simultaneously as piRNA precursors and as their only targets. Telomeric chromatin is highly sensitive to piRNA loss, implying the existence of a novel developmental checkpoint that depends on telomere integrity in the germline.

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DVE-1 is a telomere-binding protein and links the NuRD complex to telomere regulation in C. elegans

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