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

Sabrina Dietz, Miguel Vasconcelos Almeida, Emily Nischwitz, Jan Schreier, Nikenza Viceconte, Albert Fradera-Sola, Christian Renz, Alejandro Ceron-Noriega, Helle D. Ulrich, Dennis Kappei, René F. Ketting and Falk Butter ()
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Sabrina Dietz: Institute of Molecular Biology (IMB)
Miguel Vasconcelos Almeida: Institute of Molecular Biology (IMB)
Emily Nischwitz: Institute of Molecular Biology (IMB)
Jan Schreier: Institute of Molecular Biology (IMB)
Nikenza Viceconte: Institute of Molecular Biology (IMB)
Albert Fradera-Sola: Institute of Molecular Biology (IMB)
Christian Renz: Institute of Molecular Biology (IMB)
Alejandro Ceron-Noriega: Institute of Molecular Biology (IMB)
Helle D. Ulrich: Institute of Molecular Biology (IMB)
Dennis Kappei: National University of Singapore
René F. Ketting: Institute of Molecular Biology (IMB)
Falk Butter: Institute of Molecular Biology (IMB)

Nature Communications, 2021, vol. 12, issue 1, 1-20

Abstract: Abstract 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.

Date: 2021
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DOI: 10.1038/s41467-021-22861-2

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