Pia C. Maly Sundgren, 2017 Sep 12, Neuroimaging: Anatomy Meets Function. Preclinical evaluation of (111)In-DTPA-INCA-X anti-Ku70/Ku80 monoclonal 

A, Ku70/80 was purified from insect cells coinfected with recombinant baculoviruses expressing human His-Ku70 and -Ku80. Ku70/80 was incubated with PARP-1 in the presence of sonicated DNA and NAD + (lanes 1 and 3) or buffer only (lanes 2 and 4).

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. 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. 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.

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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 We (unpublished data) and others [43] had evaluated and shown that proteins involved in DNA repair including DNA-PK, p53, ATM and Ku70 had no effect on the type-I-IFN response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). Biochemical analyses of the Ku70-Ku80 het-erodimer protein demonstrated that it bound in a sequence-nonspecific fashion to virtually all double-stranded DNA ends including 5 -or3-protruding ends, blunt ends (32), and duplex DNA ending in stem–loop structures (33).

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.

DNA interaction assay. Ku70 and Ku80. Ku70 and Ku80 form a heterodimer, Ku, which possesses DNA end-binding activity (Mimori and Hardin, 1986 ).

I NHEJ katalyseras ligering av DNA-ändarna efter DNA-proteinkinas komplex (​DNA-PK katalytisk subenhet (DNA-PKcs), Ku70, Ku80) genom DNA-ligas IV i 

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. Although Ku70 is The Ku protein, a heterodimer consisting of Ku70 and Ku80 subunits, is a multifunctional complex playing critical roles in important cellular processes such as non-homologous end joining (NHEJ), V (D)J recombination, apoptosis, telomere maintenance and DNA replication (1). 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 Initially, broken DNA ends are recognized and processed, a mechanism initiated by the Ku70/80 heterodimer, which recruits DNA-dependent protein kinase and repair factor Artemis for end modification. Next, the broken DNA is ligated through a complex consisting of DNA ligase IV (Lig4), XRCC4, and Cernunnos/XLF (1). 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.

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. 1997-11-01 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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DNA interaction assay. Ku70 and Ku80. Ku70 and Ku80 form a heterodimer, Ku, which possesses DNA end-binding activity (Mimori and Hardin, 1986 ).

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. function of Ku70 at DSB sites might play a crucial role in modulating the NHEJ repair pathway [3, 14, 20, 26, 28]. There is, however, no report describing the localization and function of canine Ku70.
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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.

ku70, of the ku70/ku80 heterodimer, binds to the stem loop of tlc1, the RNA component of telomerase.