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The double-stranded DNA-binding proteins TEBP-1 and TEBP-2 form a telomeric complex with POT-1
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 proteomic...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8113555/ https://www.ncbi.nlm.nih.gov/pubmed/33976151 http://dx.doi.org/10.1038/s41467-021-22861-2 |
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author | 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, René F. Butter, Falk |
author_facet | 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, René F. Butter, Falk |
author_sort | Dietz, Sabrina |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-8113555 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-81135552021-05-14 The double-stranded DNA-binding proteins TEBP-1 and TEBP-2 form a telomeric complex with POT-1 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, René F. Butter, Falk Nat Commun Article 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. Nature Publishing Group UK 2021-05-11 /pmc/articles/PMC8113555/ /pubmed/33976151 http://dx.doi.org/10.1038/s41467-021-22861-2 Text en © The Author(s) 2021, corrected publication 2021 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article 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, René F. Butter, Falk The double-stranded DNA-binding proteins TEBP-1 and TEBP-2 form a telomeric complex with POT-1 |
title | The double-stranded DNA-binding proteins TEBP-1 and TEBP-2 form a telomeric complex with POT-1 |
title_full | The double-stranded DNA-binding proteins TEBP-1 and TEBP-2 form a telomeric complex with POT-1 |
title_fullStr | The double-stranded DNA-binding proteins TEBP-1 and TEBP-2 form a telomeric complex with POT-1 |
title_full_unstemmed | The double-stranded DNA-binding proteins TEBP-1 and TEBP-2 form a telomeric complex with POT-1 |
title_short | The double-stranded DNA-binding proteins TEBP-1 and TEBP-2 form a telomeric complex with POT-1 |
title_sort | double-stranded dna-binding proteins tebp-1 and tebp-2 form a telomeric complex with pot-1 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8113555/ https://www.ncbi.nlm.nih.gov/pubmed/33976151 http://dx.doi.org/10.1038/s41467-021-22861-2 |
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