Authors: | Hsu, H. L.; Gilley, D.; Galande, S. A.; Prakash Hande, M.; Allen, B.; Kim, S. H.; Li, G. C.; Campisi, J.; Kohwi-Shigematsu, T.; Chen, D. J. |
Article Title: | Ku acts in a unique way at the mammalian telomere to prevent end joining |
Abstract: | Telomeres are specialized DNA/protein structures that act as protective caps to prevent end fusion events and to distinguish the chromosome ends from double-strand breaks. We report that TRF1 and Ku form a complex at the telomere. The Ku and TRF1 complex is a specific high-affinity interaction, as demonstrated by several in vitro methods, and exists in human cells as determined by coimmunoprecipitation experiments. Ku does not bind telomeric DNA directly but localizes to telomeric repeats via its interaction with TRF1. Primary mouse embryonic fibroblasts that are deficient for Ku80 accumulated a large percentage of telomere fusions, establishing that Ru plays a critical role in telomere capping in mammalian cells. We propose that Ku localizes to internal regions of the telomere via a high-affinity interaction with TRF1. Therefore, Ku acts in a unique way at the telomere to prevent end joining. |
Keywords: | unclassified drug; human cell; dna-binding proteins; nonhuman; binding affinity; protein localization; animal cell; mouse; telomere; mammalia; animals; mice; cells, cultured; embryo; protein protein interaction; protein binding; in vitro study; animalia; nuclear proteins; double stranded dna; mammal; gene fusion; immunoprecipitation; fibroblast; fibroblasts; chromosome breakage; models, genetic; chromosome aberrations; protein structure; ku antigen; dna binding; dna helicases; genetic linkage; telomeric repeat binding factor 1; dna protein complex; antigens, nuclear; ku; humans; human; priority journal; article; telomeric repeat binding protein 1; trf1; protein ku 80 |
Journal Title: | Genes and Development |
Volume: | 14 |
Issue: | 22 |
ISSN: | 0890-9369 |
Publisher: | Cold Spring Harbor Laboratory Press |
Date Published: | 2000-11-15 |
Start Page: | 2807 |
End Page: | 2812 |
Language: | English |
DOI: | 10.1101/gad.844000 |
PUBMED: | 11090128 |
PROVIDER: | scopus |
PMCID: | PMC317061 |
DOI/URL: | |
Notes: | Export Date: 18 November 2015 -- Source: Scopus |