1997-11-01 · Double-strand break repair by Ku70 requires heterodimerization with Ku80 and DNA binding functions. S Jin Division of Tumor Immunology, Dana-Farber Cancer Institute, 44 Binney Street, Boston, MA 02115, USA.

Ku70 and Ku80 in A. thaliana. On the basis of their sequence similarity to the human Ku proteins, we isolated cDNAs encoding Ku70 and Ku80 homologues in this plant species (AtKu70 and AtKu80), and demonstrated that they form a functional heterodimer that both binds to double-stranded DNA and possesses DNA helicase activity. In

Our previous study with Ku70−/− and Ku80−/− mice, and cell lines has shown that Ku70- and Ku80-deficiency compromises the ability of cells to repair DNA double-strand breaks, increases radiosensitivity of cells, and Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. ku70, of the ku70/ku80 heterodimer, binds to the stem loop of tlc1, the RNA component of telomerase. Required for mating-type switching (By similarity). Complex: Ku70:Ku80 complex Macromolecular complex annotations are imported from the Complex Portal.These annotations have been derived from physical molecular interaction evidence extracted from the literature and cross-referenced in the entry, or by curator inference from information on homologs in closely related species or by inference from scientific background. The EMBO Journal Vol.16 No.22 pp.6874–6885, 1997 Double-strand break repair by Ku70 requires heterodimerization with Ku80 and DNA binding functions Shengfang Jin and David T.Weaver1 Division of The proteins Ku70 (69.8 kDa) and Ku80 (82.7 kDa) form a heterodimeric complex that is an essential component of the nonhomologous end joining DNA double-strand break repair pathway in mammalian cells. Interaction of Ku with DNA is central for the functions of Ku. 2001-03-01 · Single-stranded DNA-dependent ATP-dependent helicase.

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We find Its function remains elusive. We reisolated CLUyXIP8 by yeast two-hybrid analyses using as bait the DNA double-strand break repair protein Ku70. We show that a delayed (2–3 days), low-dose (0.02–10 Gy) IR-inducible nuclear CLUyXIP8 protein coimmunoprecipitated and colocalized (by confocal microscopy) in vivo with Ku70yKu80, a DNA The propensity for Ku70 to associate with Ku80 and to bind DNA correlates with the ability to activate DNA-PK, although two mutants showed that the roles of Ku70 in DNA-PK activation and IR repair The Ku70/80 heterodimer binds to DNA ends and attracts other proteins involved in the non-homologous end-joining (NHEJ) pathway of DNA double-strand break repair. We developed a novel assay to measure DNA binding and release kinetics using differences in Förster resonance energy transfer (FRET) of the ECFP-Ku70/EYFP-Ku80 heterodimer in soluble and DNA end bound states. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. ku70, of the ku70/ku80 heterodimer, binds to the stem loop of tlc1, the RNA component of telomerase.

Ku70/Ku80 bindet an freie DNA-Enden und ist in die Reparatur von Doppelstrangbrüchen durch die nicht-homologe Endverknüpfung involviert. 2 Genetik.

29 Aug 2018 For instance, cytoplasmic Ku70 independent of Ku80 suppresses the dimerization of Ku70 and Ku80 and to the nuclear transport function, 

The Enhanced Cyan Fluorescent Protein (ECFP)-Ku70/EYFP-Ku80 FRET Pair The Ku70/80 heterodimer binds to DNA ends as a starting point for NHEJ complex assembly and juxtaposition Both Ku70 and Ku80 therefore contain monopartite NLSs, and sequences outside the basic cluster make favorable interactions with Impα, suggesting that this may be a general feature in monopartite NLSs. We show that the Ku70 NLS has a higher affinity for Impα than the Ku80 NLS, consistent with more extensive interactions in its N-terminal region. 1997-07-01 ing of Ku70 and Ku80, which recognizes DSBs and recruits addi - tional pathway components to process and repair the Fbxo28 and Kdm2b. our study unveils a novel function for the SCF ubiquitin ligase in regulating the dynamic interaction between DNA repair machineries and DSBs.

21 Feb 2003 Arabidopsis Ku70 and Ku80 proteins form a heterodimer with DNA binding The essential role of the Ku70/Ku80 heterodimer in telomere 

DNA-PKcs is a 469-kDa protein composed of several distinct functional domains Purification of the Ku70/Ku80 dimer. Ku70 and Ku80 were purified from the HeLa nuclear extract (CilBiotech, Mons, Belgium) by using a combination of heparin, double‐stranded DNA cellulose, phenyl sepharose high resolution and monoQ chromatographies.

Function Together, Ku70 and Ku80 make up the Ku heterodimer , which binds to DNA double-strand break ends and is required for the non-homologous end joining (NHEJ) pathway of DNA repair . It is also required for V(D)J recombination , which utilizes the NHEJ pathway to promote antigen diversity in the mammalian immune system . In eukaryotes, Ku is a heterodimer comprised of two subunits, Ku70 and Ku80, that is best characterized for its central role as the initial DNA end binding factor in the "classical" non-homologous end joining (C-NHEJ) pathway, the main DNA double-strand break (DSB) repair pathway in mammals. 1997-11-17 · Abstract. Heterodimers of the 70 and 80 kDa Ku autoantigens (Ku70 and Ku80) activate the DNA-dependent protein kinase (DNA-PK). Mutations in any of the three subunits of this protein kinase (Ku70, Ku80 and DNA-PKcs) lead to sensitivity to ionizing radiation (IR) and to DNA double-strand breaks, and V(D)J recombination product formation defects.
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Our previous study with Ku70−/− and Ku80−/− mice, and cell lines has shown that Ku70- and Ku80-deficiency compromises the ability of cells to repair DNA double-strand breaks, increases radiosensitivity of cells, and Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. ku70, of the ku70/ku80 heterodimer, binds to the stem loop of tlc1, the RNA component of telomerase. Required for mating-type switching (By similarity). Complex: Ku70:Ku80 complex Macromolecular complex annotations are imported from the Complex Portal.These annotations have been derived from physical molecular interaction evidence extracted from the literature and cross-referenced in the entry, or by curator inference from information on homologs in closely related species or by inference from scientific background.

The DNA binding activity of the Ku70-Ku80 heterodimer is thought to function by LSE is an autoimmune disease, whereby the immune system mistakenly attacks healthy tissue, resulting in red rash, as a response of inflammation. Both the Ku70 and Ku80 subunits were subcloned (Reeves and Sthoeger 1989; Mimori et al. 1990), but the breakthrough occurred with the discovery Ku70 and Ku80 heterodimers function as regulatory subunits of the DNA-dependent protein kinase and play a very important role in the repairing of DNA double-strand breaks.
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also been suggested that Ku80 has a Ku70-independent DNA DSB repair function, in addition to the one depen-dent on Ku70 (Koike and Koike 2005). Throughout our several studies on supernumerary (B) chromosomes (a kind of parasitic chromosomes), we consistently came across several effects of these chromosomes in the grasshopper Eyprepocnemis

centromeric function of Ku70 was not observed in 14 other grasshopper and locust species, or in the mouse, thus suggesting that it is an autapomorphy in E. plorans. Keywords Autapomorphy.Centromere. Eyprepocnemisplorans.Geneknockdown. Immunofluorescence.Kinetochore.Ku70.Ku80.