Characterization of new telomeric proteins in C. elegans

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Telomeres are the ends of linear chromosomes and consist of repetitive double- and single-stranded DNA sequences. Telomeres are bound by dedicated protein complexes, such as shelterin in mammals, which protect telomeres from DNA damage and assist in the maintenance of telomere integrity across cell divisions. However, a comprehensive understanding of the proteins interacting with the C. elegans telomere sequence is lacking. We previously used a quantitative proteomics approach to screen for proteins binding to C. elegans telomeres, and identified TEBP-1 and TEBP-2, two paralogs that associate to telomeres in vitro and in vivo. TEBP-1 and TEBP-2 form a telomeric complex with the known single stranded telomere-binding proteins POT-1, POT-2, and MRT-1. These results define the first telomere binding complex of C. elegans, including TEBP-1 and TEBP-2, two double-stranded telomere binders, which mediate opposite telomere dynamics. In this project, we want to further characterize the organization and functionality of this C. elegans complex using biochemical and molecular biology techniques. The complex architecture will be studied by in vitro and supplemented with functional characterization in vivo using mutants. Additionally, we will characterize the additional candidates from the proteomic screen for their function at telomeres.