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. This domain only makes a small contribution to the dimer interface.

2009-03-30

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.

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

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.

2 Genetik. Der Ku70/Ku80-Komplex wird durch zwei Gene codiert: XRCC6 und XRCC5. exhibited reduced Ku80 expression.

2015-01-01

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 EMBO Journal Vol.16 No.22 pp.6874–6885, 1997 Double-strand break repair by Ku70 requires heterodimerization with Ku80 and DNA binding functions Shengfang Jin and David T.Weaver1 Division of 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 · Single-stranded DNA-dependent ATP-dependent helicase. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair.

The Ku70 and Ku80 proteins consist of three structural domains.
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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).
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The central domain of Ku70 and Ku80 is a DNA-binding beta-barrel domain. Ku makes only a few contacts with the sugar-phosphate backbone, and none with the

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 ( Ramsden and Gellert, 1998 ). 1997-11-01 · Double-strand break repair by Ku70 requires heterodimerization with Ku80 and DNA binding functions. S Jin Division of Tumor Immunology, Dana-Farber Cancer Institute, 44 Binney Street, Boston, MA 02115, USA. 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 knockout mice have 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 Ku70 forms a heterodimer with Ku80, called Ku that is well known for repairing DNA double-strand breaks through non-homologous end joining.