Please use this identifier to cite or link to this item: https://doi.org/10.1038/s41467-021-22861-2
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dc.titleThe double-stranded DNA-binding proteins TEBP-1 and TEBP-2 form a telomeric complex with POT-1
dc.contributor.authorDietz, Sabrina
dc.contributor.authorAlmeida, Miguel Vasconcelos
dc.contributor.authorNischwitz, Emily
dc.contributor.authorSchreier, Jan
dc.contributor.authorViceconte, Nikenza
dc.contributor.authorFradera-Sola, Albert
dc.contributor.authorRenz, Christian
dc.contributor.authorCeron-Noriega, Alejandro
dc.contributor.authorUlrich, Helle D.
dc.contributor.authorKappei, Dennis
dc.contributor.authorKetting, Rene F.
dc.contributor.authorButter, Falk
dc.date.accessioned2022-10-13T01:07:58Z
dc.date.available2022-10-13T01:07:58Z
dc.date.issued2021-05-11
dc.identifier.citationDietz, 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
dc.identifier.issn2041-1723
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/232746
dc.description.abstractTelomeres 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).
dc.publisherNature Research
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.sourceScopus OA2021
dc.typeArticle
dc.contributor.departmentBIOCHEMISTRY
dc.description.doi10.1038/s41467-021-22861-2
dc.description.sourcetitleNature Communications
dc.description.volume12
dc.description.issue1
dc.description.page2668
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