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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. Although Ku70 is proposed as a candidate for a tumor suppressor gene, not many da Ku70/Ku80 ist ein heterodimerer Proteinkomplex. Ku70/Ku80 bindet an freie DNA-Enden und ist in die Reparatur von Doppelstrangbrüchen durch die nicht-homologe Endverknüpfung involviert. 2 Genetik. Der Ku70/Ku80-Komplex wird durch zwei Gene codiert: XRCC6 und XRCC5.
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However, it is not yet clear whether KARP-1 forms a heterodimer with Ku70 and works as a heterodimer. factors, including Ku70, Ku80, XRCC4, and Lig4 (Taccioli et al., 1994; Li et al., 1995; Gu et al., 1997; Frank et al., 1998). Ku70 and Ku80 form the “Ku” DNA end-binding complex which functions as the DSB recognition com-ponent of C-NHEJ, whereas the XRCC4/ Lig4 complex is specific for C-NHEJ ligation. (2002) Korabiowska et al.
This complex plays a key role in DNA repair due to its ability to bind DNA double-strand breaks and facilitate repair by the nonhomolo-gous end-joining pathway. Ku70 and Ku80 have been proposed to contain DNA-PKcs functions both within and outside of the damage response to effectively design therapeutic strategies. Ku70 and Ku80 (also called Ku86) are encoded by the XRCC6 and XRCC5 genes, respectively, in humans, and have a strong affi nity for free ends of DNA ( 21 ).
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.
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. Ku, the heterodimer of Ku70 and Ku80, plays an essential role in the DNA double-strand break (DSB) repair pathway, i.e., non-homologous end-joining (NHEJ). Two isoforms of Ku80 encoded by the same genes, namely, Ku80 and KARP-1 are expressed and function in primate cells, but not in rodent cells.
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
Ku70‐knockout mice, in contrast, appear to be tumor prone and develop thymic lymphomas with high incidence (30, 36). Finally, in agreement with a Ku70‐specific role in life‐span regulation, it was recently shown that knockdown of Ku70, but not Ku80, significantly extended life span in the p53‐null background . XRCC4, is a protein of unknown function. The Ku70 protein is an additional component of DNA-PK; Ku70 forms a het-erodimer with Ku80 to generate the DNA end-binding com-ponent of the enzyme.
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.
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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 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 Ku70 and Ku80 proteins consist of three structural domains. The N-terminal domain is an alpha/beta domain. This domain only makes a small contribution to the dimer interface.
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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. Microtubules.Orthoptera.RNAi.Spindleassembly checkpoint Abbreviations
However, it also functions in maintenance of telomeres, chromosome 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. The domain structure of zebrafish Ku80 protein is similar to that of other vertebrate Ku80 and Ku70 proteins ( Figure 2A). When compared with Ku80 in other vertebrates, zebrafish Ku80 is most closely related to pufferfish, but has >50% identity to Ku80 in more distantly related mammalian species ( Figure 2B , 2C ). KU70 and KU80 as top hits.
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LRIK interacts with the Ku70-Ku80 heterodimer enhancing the efficiency of NHEJ repair Despite recent advances in our understanding of the function of long noncoding RNAs (lncRNAs), their roles and functions in DNA repair pathways remain poorly understood.
2015-01-01 1997-11-17 Ku80 is best known for its function in DNA damage repair in its heterodimer with Ku70 [20], while accumulating evidence has suggested that Ku80 also plays important roles in cellular processes 2005-01-01 Ku, the heterodimer of Ku70 and Ku80, plays an essential role in the DNA double-strand break (DSB) repair pathway, i.e., non-homologous end-joining (NHEJ). Two isoforms of Ku80 encoded by the same genes, namely, Ku80 and KARP-1 are expressed and function in primate cells, but not in rodent cells. 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.