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.

suggest that the binding of the Ku80 and Ku70 proteins to DNA plays an important role in the joining of both signal and coding ends. On the other hand, the scid

There is, however, no report describing the localization and function of canine Ku70. In this study, we have cloned Ku70 cDNA from a beagle dog testis library and conducted comparative analysis to understand the Ku70 is the 70 kDa subunit of the lupus Ku autoantigen. The lupus Ku autoantigen was identified in individuals with systemic lupus erythematosus (SLE) and related disorders. The Ku antigen is a heterodimer of Ku70 and Ku80. The Ku70/Ku80 complex functions as a single-stranded DNA-dependent ATP-dependent helicase. 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).

Ku70 and ku80 function

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. 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 Ku70 and Ku80 proteins consist of three structural domains. The N-terminal domain is an alpha/beta domain.

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 is thought to function as a molecular scaffold to which other proteins involved in NHEJ can bind, orienting the double-strand break for ligation.

Ku80 works as a heterodimer with Ku70. 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. 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 Ku70 and Ku80 proteins; X-ray crystallography Ku70 and Ku80 form a heterodimeric complex involved in multiple nuclear processes.
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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.

1 Oct 2019 In the present study, to evaluate the role of Ku80 in thyroid carcinoma (TC), For example, the expression of Ku70/Ku80 has been shown to be 26 Mar 2002 These results suggest that the evolutionarily conserved Ku70–Ku80 heterodimer functions in DSB repair by the NHEJ pathway in A. thaliana.
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1997-07-01

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.