2009-03-30

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.

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). 2011-01-12 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 Ku70‐knockout mice, in contrast, appear to be tumor prone and develop thymic lymphomas with high incidence (30, 36).

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2011-10-01 · 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. 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.

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

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).

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). 2011-01-12 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.

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 ). DNA-PKcs is a 469-kDa protein composed of several distinct functional domains

We further defined the function of the Ku70 and Ku80 C-terminal domains in DNA end binding and DNA-PKCS interaction. 2. Results 2.1.

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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Heterodimers of the 70 and 80 kDa Ku autoantigens (Ku70 and Ku80) activate the DNA‐dependent protein kinase (DNA‐PK).

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

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).