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Importantly, to determine downstream mechanisms, epistasis experiments were performed, and data indicated that ELO3 and YKU70/80 share a common pathway for the regulation of telomere length. More specifically, chromatin immunoprecipitation assays revealed that the telomere binding and protective function of YKu80p in vivo was reduced in elo3Delta cells, whereas its non-homologues end-joining function was not altered.

Here, we identify eight lysines in Ku70 that are targets for acetylation in vivo. Five of these, K539 Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Ku70 + Ku80 antibody (ab53126) ab53126 at 1/50 dilution staining Ku70 + Ku80 in human breast carcinoma by Immunohistochemistry, Paraffin embedded tissue in the absence and … 2013-02-06 The Ku70 protein is involved in numerous cell functions, the nonhomologous end joining (NHEJ) DNA repair pathway being the best known. Here, we report a novel function for this protein in the grasshopper Eyprepocnemis plorans . Ku70/Ku80 Antibodies The protein encoded by this gene is the 80-kilodalton subunit of the Ku heterodimer protein which is also known as ATP-dependant DNA helicase II or DNA repair protein XRCC5. XRCC5 (X-Ray Repair Cross Complementing 5) is a Protein Coding gene. Diseases associated with XRCC5 include Viral Exanthem and Werner Syndrome.Among its related pathways are Cytosolic sensors of pathogen-associated DNA and DNA damage_NHEJ mechanisms of DSBs repair.Gene Ontology (GO) annotations related to this gene include transcription regulatory region DNA binding. Ku70 (also known as XRCC6 Structural analysis of the Ku70/80 heterodimer bound to DNA indicates that subunit contacts lead to the formation of a highly charged channel through which the DNA passes without making any contacts with the DNA bases .

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. The Ku70/80 heterodimer binds to DNA ends with high affinity and specificity. The protein forms a ring that can thread onto a DNA end, which explains its inability to bind to circular DNA molecules or internal positions on the chromosome . Once bound to DNA, Ku70/80 attracts the catalytic subunit of the DNA-dependent protein kinase (DNA-PK CS). 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.

Request PDF | KARP-1 works as a heterodimer with Ku70, but the function of KARP-1 cannot perfectly replace that of Ku80 in DSB repair | Ku, the heterodimer of Ku70 and Ku80, plays an essential

The connection between the Ku70 level and stabilization of β-catenin merits further investigation, which could shed light on possible ways to enhance pancreatic β-cell proliferation. It is known that Ku70/80 has a high affinity for DNA ends; therefore, to exclude the possibility that the increase in 12/23 regulation was an artifact due to binding and translocation of Ku70/80 into the DNA, we performed experiments with supercoiled circular DNA. Ku70, a known nonhomologous end-joining (NHEJ) factor, also functions in tumor suppression, although this molecular mechanism remains uncharacterized.

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The aberrant expression and localization of these proteins fail to control DNA repair and apoptosis. sClusterin is the Ku70 partner that sterically inhibits Bax-dependent cell death after damage in some pathologic conditions. The protein encoded by this gene is the 80-kilodalton subunit of the Ku heterodimer protein which is also known as ATP-dependant DNA helicase II or DNA repair protein XRCC5. Ku is the DNA-binding component of the DNA-dependent protein kinase, and it functions together with the DNA ligase IV-XRCC4 complex in the repair of DNA double-strand break by non-homologous end joining and Suppression of Ku70/80 or Lig4 leads to decreased stable transformation and enhanced homologous recombination in rice AyakoNishizawa-Yokoi1,SatokoNonaka1,2,HiroakiSaika1,Yong-IkKwon1,3,KeishiOsakabe1,4 andSeiichiToki1,3 Ku80 is a protein that, in humans, is encoded by the XRCC5 gene.

Ku70, a known nonhomologous end-joining (NHEJ) factor, also functions in tumor suppression, although this molecular mechanism remains uncharacterized. 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). Accordingly, these results may be attributed to a decrease in protein levels of both OsKu80 and OsKu70 caused by the down‐regulation of the expression of OsKu80 mRNA in KD‐Ku80 rice calli The Ku70/80 heterodimer binds to DNA ends with high a nity and speciﬁcity.
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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). Accordingly, these results may be attributed to a decrease in protein levels of both OsKu80 and OsKu70 caused by the down‐regulation of the expression of OsKu80 mRNA in KD‐Ku80 rice calli The Ku70/80 heterodimer binds to DNA ends with high a nity and speciﬁcity. The protein forms a ring that can thread onto a DNA end, which explains its inability to bind to circular DNA molecules or internal positions on the chromosome [5].

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The Ku70/80 heterodimer rapidly responds to DSBs, stimulating recruitment of downstream NHEJ factors to protect, process, and ligate broken DNA ends. Work in our lab has shown that a D192A/D195R mutation in helix five of the Ku70 von Willebrand A (vWA) domain leads to an NHEJ defect. However, little is known about the function of this region in NHEJ.

More specifically, chromatin immunoprecipitation assays revealed that the telomere binding and protective function of YKu80p in vivo was reduced in elo3Delta cells, whereas its non-homologues end-joining function was not altered. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection.

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 transformation test veriﬁed that Ku70 was immunoprecipitated using 0.5mg Hela whole cell extract, 5µg of Rabbit polyclonal to Ku70 and 50µl of protein G magnetic beads (+). No antibody was added to the control (-). The antibody was incubated under agitation with Protein G beads for 10min, Hela whole cell extract lysate diluted in RIPA buffer was added to each sample and incubated for a further 10min under agitation. functions related to the stability of chromosomes in mammalian cells.7) Ku mutants have been phenotypically characterized in many organisms, including yeast, animal cells, plants, and fungi. In yeast Saccharomyces cerevisiae Ku Ku70/80 C-terminalarm; and positions 618 Suppression of Ku70/80 or Lig4 leads to decreased stable transformation and enhanced homologous recombination in rice AyakoNishizawa-Yokoi1,SatokoNonaka1,2,HiroakiSaika1,Yong-IkKwon1,3,KeishiOsakabe1,4 andSeiichiToki1,3 1Plant Genome Engineering Research Unit, National Institute of Agrobiological Sciences, 2-1-2 Kannondai, Tsukuba, Ibaraki, 305-8602, Japan; 2Graduate … 2007-01-23 The Ku70/80 complex recognizes DNA breaks and serves as an essential hub for recruitment of NHEJ components. The localization of the SAP domain in the DNA aperture suggests a function as a flexible entry gate for broken DNA. Databases.

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