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Telomeres are bound by dedicated proteins, which protect them from DNA damage and regulate telomere length homeostasis. In the nematode  Caenorhabditis elegans , a comprehensive understanding of the proteins interacting with the telomere sequence is lacking. Here, we harnessed a quantitative proteomics approach to identify TEBP-1 and TEBP-2, two paralogs expressed in the germline and embryogenesis that associate to telomeres in vitro and in vivo.  tebp-1  and  tebp-2  mutants display strikingly distinct phenotypes:  tebp-1  mutants have longer telomeres than wild-type animals, while  tebp-2  mutants display shorter telomeres and a Mortal Germline. Notably,  tebp-1;tebp-2  double mutant animals have synthetic sterility, with germlines showing signs of severe mitotic and meiotic arrest. Furthermore, we show that POT-1 forms a telomeric complex with TEBP-1 and TEBP-2, which bridges TEBP-1/-2 with POT-2/MRT-1. These results provide insights into the composition and organization of a telomeric protein complex in  C. elegans .

The double-stranded DNA-binding proteins TEBP-1 and TEBP-2 form a telomeric complex with POT-1