Repository logo
 

The double-stranded DNA-binding proteins TEBP-1 and TEBP-2 form a telomeric complex with POT-1.

Published version
Peer-reviewed

Loading...
Thumbnail Image

Type

Article

Change log

Authors

Almeida, Miguel Vasconcelos  ORCID logo  https://orcid.org/0000-0002-4816-3111
Nischwitz, Emily 
Schreier, Jan 

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.

Description

Keywords

Germ Cells, Telomere, Animals, Animals, Genetically Modified, Caenorhabditis elegans, Multiprotein Complexes, DNA-Binding Proteins, Telomere-Binding Proteins, Caenorhabditis elegans Proteins, Protein Isoforms, DNA, Microscopy, Fluorescence, Phylogeny, Binding Sites, Base Sequence, Protein Binding, Mutation

Journal Title

Nature communications

Conference Name

Journal ISSN

2041-1723

Volume Title

12

Publisher

Sponsorship
NIH HHS (P40 OD010440)