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Title: | The double-stranded DNA-binding proteins TEBP-1 and TEBP-2 form a telomeric complex with POT-1 | Authors: | Dietz, Sabrina Almeida, Miguel Vasconcelos Nischwitz, Emily Schreier, Jan Viceconte, Nikenza Fradera-Sola, Albert Renz, Christian Ceron-Noriega, Alejandro Ulrich, Helle D. Kappei, Dennis Ketting, Rene F. Butter, Falk |
Issue Date: | 11-May-2021 | Publisher: | Nature Research | Citation: | Dietz, Sabrina, Almeida, Miguel Vasconcelos, Nischwitz, Emily, Schreier, Jan, Viceconte, Nikenza, Fradera-Sola, Albert, Renz, Christian, Ceron-Noriega, Alejandro, Ulrich, Helle D., Kappei, Dennis, Ketting, Rene F., Butter, Falk (2021-05-11). The double-stranded DNA-binding proteins TEBP-1 and TEBP-2 form a telomeric complex with POT-1. Nature Communications 12 (1) : 2668. ScholarBank@NUS Repository. https://doi.org/10.1038/s41467-021-22861-2 | Rights: | Attribution 4.0 International | 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. © 2021, The Author(s). | Source Title: | Nature Communications | URI: | https://scholarbank.nus.edu.sg/handle/10635/232746 | ISSN: | 2041-1723 | DOI: | 10.1038/s41467-021-22861-2 | Rights: | Attribution 4.0 International |
Appears in Collections: | Elements Staff Publications |
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