The double-stranded DNA-binding proteins TEBP-1 and TEBP-2 form a telomeric complex with POT-1.
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Authors
Nischwitz, Emily
Schreier, Jan
Renz, Christian
Ceron-Noriega, Alejandro
Ulrich, Helle D
Publication Date
2021-05-11Journal Title
Nat Commun
ISSN
2041-1723
Publisher
Springer Science and Business Media LLC
Volume
12
Issue
1
Language
en
Type
Article
This Version
VoR
Metadata
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Dietz, S., Almeida, M. V., Nischwitz, E., Schreier, J., Viceconte, N., Fradera-Sola, A., Renz, C., et al. (2021). The double-stranded DNA-binding proteins TEBP-1 and TEBP-2 form a telomeric complex with POT-1.. Nat Commun, 12 (1) https://doi.org/10.1038/s41467-021-22861-2
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.
Keywords
Article, /631/45/475, /631/80/103/560, /82/80, /82/83, /82/111, /82/58, /14/19, /14/32, /14/63, /38/23, /38/35, /38/70, /64/11, article
Sponsorship
Deutsche Forschungsgemeinschaft (German Research Foundation) (407023052/GRK2526/1, 393547839 – SFB 1361)
Identifiers
s41467-021-22861-2, 22861
External DOI: https://doi.org/10.1038/s41467-021-22861-2
This record's URL: https://www.repository.cam.ac.uk/handle/1810/329852
Rights
Licence:
http://creativecommons.org/licenses/by/4.0/
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