(Abstract); Kuci V, Nordström L, Jerkeman M, Ek S (2015) Emerging role of of 111In-DTPA-INCA-X anti-Ku70/Ku80 monoclonal antibody in prostate cancer.

The Ku70/Ku80 heterodimer has ATP-dependent DNA helicase activity and functions as the DNA-binding regulatory component of DNA-dependent protein kinase (DNA-PK) (6-8). The assembly of the DNA-PK complex at DNA ends is required for nonhomologous end-joining (NHEJ), one mechanism involved in double-stranded DNA break repair and V(D)J recombination (8).

Interaction of Ku with DNA is central for the functions of Ku. 2001-03-01 · Single-stranded DNA-dependent ATP-dependent helicase. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair. When associated with KU80, binds to double-stranded telomeric and non-telomeric DNA sequences, but not to single-stranded DNA. Ku80 is a protein that, in humans, is encoded by the XRCC5 gene. 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. 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.

The Ku70/Ku80 complex functions as a single-stranded DNA-dependent ATP-dependent helicase. 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.

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.

Protection of Kidney Function with Human Antioxidation Protein Preclinical evaluation of (111)In-DTPA-INCA-X anti-Ku70/Ku80 monoclonal antibody in

When associated with KU80, binds to double-stranded telomeric and non-telomeric DNA sequences, but not to single-stranded DNA. Ku80 is a protein that, in humans, is encoded by the XRCC5 gene. 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. 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.

14 Sep 2020 of the Ku70/80 heterodimer in vitro. We further defined the function of the Ku70 and Ku80 C-terminal domains in DNA end binding and

First, either Ku70 or Ku80 functions outside the Ku heterodimer such that deletion of one is not identical to deletion of the other. Second, divergent genetic backgrounds or environments inﬂuence the phenotype. To distinguish between these possi-bilities, the Ku70 and Ku80 mutations were crossed together to generate Ku70, Ku80, and double-mutant mice The Ku heterodimer, comprised of Ku70 and Ku80 subunits, is a conserved complex involved in nonhomologous end-joining (NHEJ). 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).

Purified Ku protein was found to promote the association of two DNA molecules in vitro; thus, it was proposed to possess end bridging or alignment activity ( … We conclude that Ku70 and Ku80 may have functions in V (D)J recombination and DNA repair that are independent of DNA-PKcs. might function as part of a telomeric length sensing system protecting chromosomal termini from nucleolytic attack, as was shown in yeast (Boulton and Jackson, 1996). Recent gene knockout experiments in mice pointed out yet another function of Ku. As expected, both Ku70 and Ku80 … The Ku70–Ku80 heterodimer of other species binds to the termini of double‐stranded DNA as the initial step in DSB repair. To determine whether the AtKu70–AtKu80 heterodimer also binds to DNA fragments, we performed EMSA analysis with the recombinant proteins produced in E. coli . Purification of the Ku70/Ku80 dimer.
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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.

Immunofluorescence.Kinetochore.Ku70.Ku80. Microtubules.Orthoptera.RNAi.Spindleassembly checkpoint Abbreviations Ku70 and Ku80.
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1 Oct 2018 Key Words: Ku70SHP-1SIRT1DNA damage repairNon-homologous end joining or DNA-targeting heterodimer (KU70 and KU80) are more sensitive to DNA To investigate the role of KU70 in response to DNA damage, we

As a result, deletion of either causes a very similar The Ku70–Ku80 heterodimer of other species binds to the termini of double‐stranded DNA as the initial step in DSB repair. To determine whether the AtKu70–AtKu80 heterodimer also binds to DNA fragments, we performed EMSA analysis with the recombinant proteins produced in E. coli . Ku70 is an evolutionarily conserved protein that has functions in DNA repair and maintenance [96]. It is a heterodimeric protein made up of Ku70 and Ku80 [97] . We (unpublished data) and others [43] had evaluated and shown that proteins involved in DNA repair including DNA-PK, p53, ATM and Ku70 had no effect on the type-I-IFN response induced by cytosolic dsDNA stimulation. There was no correlation between the transcript levels of Ku80 and LUC luminescence derived from T‐DNA stable transformation in KD‐OsKu80 rice calli (Figs 1b, 2d,e). It has been shown that the Ku70/80 protein functions as a heterodimer to repair DSBs, with the two constituents stabilizing each other (Smider et al., 1994).