Abstract In this study, the ku70 and ku80 homologs from the Aspergillus niger genome were identiﬁed and their function was analyzed using targeted mutagenesis. The role of the ku80 gene in non-homologous end-joining (NHEJ) was investigated by calculating the frequency of homolo-gous recombination. The transformation test veriﬁed that

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.

The data from Bennett et al. is consistent with the crystal structure as determined by Walker et al. (2001) and further clarifies previous conclusions about the role of Ku70/80 tied to its structure. 2015-01-01 · Ku has been suggested to function in base excision repair (BER), which repairs DNA base damage, apurinic/apyrimidic (AP) sites and single-strand breaks (SSBs) . Cells deficient in Ku70 and Ku80 were sensitive to reactive oxygen species (ROS) and alkylation damage producing agents that result in base lesions and SSBs .

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The Journal of Experimental Medicine 18 maj 2015. NF-κB is lersta Norrland i mitten på 80-talet, första respektive International Index of Erectile Function (IIEF)-for- Ku70, fosforylerade DNA-PKcs och PAR mättes. Arbetet resulterade i prop. 1979/80.'10 om kontroll av hybrid—DNA-teknikens av propositionen hemställde socialut- skottet i betänkandet SoU 1979/80:18 att Marja-Leena Ojutkangas, leg sjuksköt, forskningsassistent (80 %) Functional performance in self-care and mobility after selective dorsal rhizotomy: a 10-year practice-based Decreased Ku70 Levels in Prostate Cancer. 80 This data is consistent with the findings of Dangi-Garimella et al. cancer samples, 13 suggesting an anti-metastatic function in prostate cancer as well.

We propose a structural model of the functions of the subunit‐specific C‐terminal domains in the context of the full‐length Ku70–Ku80 protein . The Ku70‐SAP domain changes its position on DNA binding from the base of the α/β domain of Ku80 to a position that might be proximal to the ring in the side of Ku that faces the continuous DNA.

The N-terminal domain is an alpha/beta domain. This domain only makes a small contribution to the dimer interface. Ku70/80 is an heterodimeric factor that plays a critical role in the repair of double strand breaks by non-homologous end joining (NHEJ).

Abstract In this study, the ku70 and ku80 homologs from the Aspergillus niger genome were identiﬁed and their function was analyzed using targeted mutagenesis. The role of the ku80 gene in non-homologous end-joining (NHEJ) was investigated by calculating the frequency of homolo-gous recombination. The transformation test veriﬁed that

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. EM maps have been deposited in EMDB (EMD‐11933). Coordinates have been deposited in Protein Data Bank Ku70 is known as the key component of classic NHEJ that plays a critical role in detecting DSBs (Puebla-Osorio et al., 2014).

(2001) and further clarifies previous conclusions about the role of Ku70/80 tied to its structure.
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1999-01-01 Invitrogen Anti-Ku70/Ku80 Monoclonal (162), Catalog # MA1-21818. Tested in Immunofluorescence (IF), Immunocytochemistry (ICC), Immunohistochemistry (Paraffin) (IHC (P)) and Flow Cytometry (Flow) applications. This antibody reacts with Human, Mouse, Non-human primate, Rat, Xenopus laevis samples. Supplied as 500 µL purified antibody (0.2 mg/mL). The Ku70/80 heterodimer rapidly responds to DSBs, stimulating recruitment of downstream NHEJ factors to protect, process, and ligate broken DNA ends.

2012-02-10 2013-07-01 2004-07-09 KU70 – Kontrolluppgift – Näringsbidrag och royalty (SKV 2316) På skatteverket.se använder vi kakor (cookies) för att webbplatsen ska fungera på ett bra sätt för dig. Genom att surfa vidare godkänner du att vi använder kakor. 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).
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Marja-Leena Ojutkangas, leg sjuksköt, forskningsassistent (80 %) Functional performance in self-care and mobility after selective dorsal rhizotomy: a 10-year practice-based Decreased Ku70 Levels in Prostate Cancer.

However, how Ku70/80 operates at telomere seems to differ among species. Ku70/80 associates with telomeric DNA ( 13) and binds to TRF1 and TRF2 ( 14, 15). Moreover, Ku has been reported to associate with hTERT and telomerase activity ( 16).

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Cancer control and functional. outcomes after radical KASTRATION MINSKAR Ku70-NIVÅERNA I PROSTATACANCERCELLER. Al-Ubaidi, F. 1 Motsvarande data för cT2 var: pT1-23 (15%), pT2-80 (42%) och. 98 (65%) för pT3-4.

Concomitantly, DNA-bound Ku70/80 proteins serve as a docking platform for sequential binding of C-NHEJ components and for an array of proteins mediating the DNA-damage response. Further, Ku70/80 have been reported to coordinate DSB repair with cell cycle arrest, pathway choice, and, if needed, apoptosis. Molecular Function; ATP binding; DNA helicase activity; damaged DNA binding; telomerase RNA binding; telomeric DNA binding; Biological Process; double-strand break repair via nonhomologous end joining; recombinational repair; telomere maintenance; Cellular Component; Ku70:Ku80 complex 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.