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

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.