Please use this identifier to cite or link to this item:
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.
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
ISSN: 2041-1723
DOI: 10.1038/s41467-021-22861-2
Rights: Attribution 4.0 International
Appears in Collections:Elements
Staff Publications

Show full item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
10_1038_s41467-021-22861-2.pdf7.15 MBAdobe PDF




checked on Nov 21, 2022

Page view(s)

checked on Nov 24, 2022

Google ScholarTM



This item is licensed under a Creative Commons License Creative Commons