ArticleCell research2017
Structure of the fission yeast S. pombe telomeric Tpz1-Poz1-Rap1 complex.
Article in Cell research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 22 citations in OpenAlex.
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- Nuclear genome organization in fungi: from gene folding to Rabl chromosomes.FEMS microbiology reviews · 2023Article
- Telomeres and Their Neighbors.Genes · 2022Review
- Structural insights into Pot1-ssDNA, Pot1-Tpz1 and Tpz1-Ccq1 Interactions within fission yeast shelterin complex.PLoS genetics · 2022Article
- The evolution of metazoan shelterin.Genes & development · 2021Article
- Ccq1-Raf2 interaction mediates CLRC recruitment to establish heterochromatin at telomeres.Life science alliance · 2021Article
- Crystal structure ofJournal of advanced research · 2020Article
- Telomere-binding proteins Taz1 and Rap1 regulate DSB repair and suppress gross chromosomal rearrangements in fission yeast.PLoS genetics · 2019Article
- Casein kinase 2 regulates telomere protein complex formation through Rap1 phosphorylation.Nucleic acids research · 2019Article
- TRFH domain: at the root of telomere protein evolution?Cell research · 2018Article
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10 authors at 6 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Telomeric shelterin complex caps chromosome ends and plays a crucial role in telomere maintenance and protection. In the fission yeast Schizosaccharomyces pombe, shelterin is composed of telomeric single- and double-stranded DNA-binding protein subcomplexes Pot1-Tpz1 and Taz1-Rap1, which are bridged by their interacting protein Poz1. However, the structure of Poz1 and how Poz1 functions as an interaction hub in the shelterin complex remain unclear. Here we report the crystal structure of Poz1 in complex with Poz1-binding motifs of Tpz1 and Rap1. The crystal structure shows that Poz1 employs two different binding surfaces to interact with Tpz1 and Rap1. Unexpectedly, the structure also reveals that Poz1 adopts a dimeric conformation. Mutational analyses suggest that proper interactions between Tpz1, Poz1, and Rap1 in the shelterin core complex are required for telomere length homeostasis and heterochromatin structure maintenance at telomeres. Structural resemblance between Poz1 and the TRFH domains of other shelterin proteins in fission yeast and humans suggests a model for the evolution of shelterin proteins.
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