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Isolation of Ku70-binding proteins (KUBs).

Nucleic acids research | May 15, 1999

http://www.ncbi.nlm.nih.gov/pubmed/10219089

DNA-dependent protein kinase (DNA-PK) plays a critical role in resealing DNA double-stand breaks by non-homologous end joining. Aside from DNA-PK, XRCC4 and DNA ligase IV, other proteins which play a role(s) in this repair pathway remain unknown; DNA-PK contains a catalytic subunit (DNA-PKcs) and a DNA binding subunit (Ku70 and Ku80). We isolated Ku70-binding proteins (KUB1-KUB4) using yeast two-hybrid analyses. Sequence analyses revealed KUB1 to be apolipoprotein J (apoJ), also known as X-ray-inducible transcript 8 (XIP8), testosterone-repressed prostate message-2 (TRPM-2) and clusterin. KUB2 is Ku80. KUB3 and KUB4 are unknown, >10 kb trans-cripts. Interactions of apoJ/XIP8 or KUB3 with Ku70 were confirmed by co-immunoprecipitation analyses in MCF-7:WS8 breast cancer or IMR-90 normal lung fibroblast cells, respectively. The interaction of apoJ/XIP8 with Ku70 was confirmed by far-western analyses. Stable over-expression of full-length apoJ/XIP8 in MCF-7:WS8 caused decreased Ku70/Ku80 DNA end binding that was restored by apoJ/XIP8 monoclonal antibodies. The role of apoJ/XIP8 in ionizing radiation resistance/sensitivity is under investigation.

Pubmed ID: 10219089 RIS Download

Mesh terms: Animals | Antigens, Nuclear | Base Sequence | Carrier Proteins | Cell Line | Cloning, Molecular | Clusterin | DNA Helicases | DNA Probes | DNA Repair | DNA-Activated Protein Kinase | DNA-Binding Proteins | Glycoproteins | Humans | Mice | Molecular Chaperones | Nuclear Proteins | Protein Binding | Protein-Serine-Threonine Kinases | Recombinant Proteins | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Tumor Cells, Cultured

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Associated grants

  • Agency: NCI NIH HHS, Id: CA-50595
  • Agency: NCI NIH HHS, Id: CA-ES78530
  • Agency: NCI NIH HHS, Id: CA50519
  • Agency: NCI NIH HHS, Id: R01 CA139217

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