Ku protein

KU80; Ku-core domain, Ku80 subfamily; Ku80 is a subunit of the Ku protein, which plays a key role in multiple nuclear processes such as DNA repair, chromosome maintenance, transcription regulation, and V (D)J recombination. The mechanism underlying the ... pfam08785. Location:558 → 672.

Ku protein. The Ku protein was initially identified by Mimori et al. as the antigen of the autoantibody in a patient of an autoimmune disease, polymyositis-scleroderma overlap . Subsequent studies showed that the Ku protein consists of two polypeptides of 70 kDa and 80 kDa, ...

The Ku autoantigen is a heterodimer of 70 (p70) and approximately 80 kDa (p80) subunits that is the DNA-binding component of the DNA-dependent protein kinase (DNA-PK) complex involved in DNA ...

Ku is a dimeric protein complex that binds to DNA double-strand break ends and is required for the non-homologous end joining (NHEJ) pathway of DNA repair. Ku is evolutionarily conserved from bacteria to humans. The ancestral bacterial Ku is a homodimer (two copies of the same protein bound to each other). [2]Background and purpose: Ku70 and Ku86, multifunctional DNA repair proteins, bind to broken DNA ends, including double-strand breaks, and trigger a DNA repair pathway. To investigate the involvement of these proteins in DNA fragmentation after ischemia/reperfusion, Ku protein expression was examined before and after transient focal cerebral ischemia (FCI) in mice.Here we address how the nature of a protein obstruction dictates how Ku interacts with a DNA end. Ku is unable to access the ends within an important intermediate in V(D)J recombination (a complex of RAG proteins bound to cleaved recombination targeting signals), but Ku readily displaces the linker histone, H1, from DNA.DNA-dependent protein kinase catalytic subunit (DNA-PKcs) is a member of the phosphatidylinositol 3-kinase related kinase family, which can phosphorylate more than 700 substrates. As the core enzyme, DNA-PKcs forms the active DNA-PK holoenzyme with the Ku80/Ku70 heterodimer to play crucial roles in cellular DNA damage response (DDR). Once DNA double strand breaks (DSBs) occur in the cells, DNA ...1 day ago · Small cell protein, a mitotic inhibitor kinase. XIAP. Inhibitor of apoptosis, x-linked. YAP. Yes-associated protein 1. Zap-70. z-chain-associated protein kinase. 修订时间 2007 年 5 月. 蛋白、信号通路和抗体首字母缩写按字母排序,由 Cell Signaling Technology 组织完成。.Besides these inhibiting molecules, HDR can also be promoted using small interfering RNA (siRNA) to inhibit the expression of Ku protein, which is the pioneer protein in the NHEJ pathway. Li et al. assessed this method on pig fetal fibroblasts (Li et al., 2018). The result showed that by inhibiting Ku70 or Ku80 expression, HR can be promoted by ...

Feb 26, 2010 · The repair of DNA double-strand breaks (DSBs) is critical for the maintenance of genomic integrity and viability for all organisms. Mammals have evolved at least two genetically discrete ways to mediate DNA DSB repair: homologous recombination (HR) and non-homologous end joining (NHEJ). Here, the double-strand breaks are primarily detected by Ku protein (Ku70-Ku80 heterodimer) [117], which then recruits the DNA protein kinase catalytic subunits (DNA-PKcs), forming Ku-DNA-PK complex surrounding the broken strands. When a double-strand break occurs, the configuration at the broken ends can vary. They can have blunt ends, 5 ...Ku protein, a heterodimer of 70 kDa and 83 kDa polypeptides, is the regulatory component of the DNA-dependent protein kinase (DNA-PK). Ku protein binds to DNA discontinuities and is essential for DNA double-strand break repair.The Ku heterodimer is a well conserved protein(s), with homologs known to exist in every species from bacteria to humans . In all organisms examined, mutations in either Ku subunit result in the expected deficits in DNA DSB repair, DNA recombination, and sensitivities to DNA-damaging agents. Importantly, in all organisms, with one glaring ...KU80 was one of the first radiosensitivity genes discovered from such studies (Taccioli et al., 1994 ). Its function is to protect the ends of DNA from further degradation and, importantly, to recruit the protein kinase DNA-PKcs (DNA-dependent protein kinase catalytic subunit (officially known as PRKDC)).

39 Citations. 69 Altmetric. Metrics. Abstract. The DNA-dependent protein kinase (DNA-PK), which comprises the KU heterodimer and a catalytic subunit (DNA …Ku is a heterodimeric protein composed of approximately 70- and approximately 80-kDa subunits (Ku70 and Ku80) originally identified as an autoantigen recognized by the sera of patients with autoimmune diseases. Ku has high binding affinity for DNA ends and that is why originally it was known as a DNA end binding protein, but now it is known to ...Conventionally, KU complex, the regulatory subunit of DNA-dependent protein kinase (DNA-PK), together with the catalytic subunit of DNA-PK (DNA-PKcs), mediates DNA damage repair in the nucleus. Here, we found KU complex abundantly expressed in the cytoplasm, where it recognized accumulated cytoplasmic DNA in aged human and mouse CD4 + T cells ...Although all structural studies of DNA-PK contain the same full-length DNA-PKcs, different constructs of Ku protein are used in the complexes defined by X-ray and cryo-EM studies. The X-ray structure of DNA-PK contains Ku80CTR (Sibanda et al., 2017), while two cryo-EM studies contain full length Ku70/80 (Sharif et al., 2017; Yin et al., 2017 ...Sep 1, 1999 · The level of Ku protein was assessed by Western blot with anti-Ku antiserum in cytoplasmic, nuclear, and whole-cell extracts from unstimulated or activated B cells. One representative datum from six comparable experiments is shown. (B) Ku fails to associate with CD40 in B cells following stimulation that induces IgCS. Membrane/cytoplasmic ...The dissection of the Ku protein from eukaryotes and prokaryotes into individual domains described above suggests an evolutionary scenario for these proteins. The Ku core is an ancient domain that was probably present in bacteria and archea even before the advent of the eukaryotes. There are clear indications that, in these organisms, the Ku ...

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Although Ku80 requires Ku70 for binding to DNA, Ku70 may display some weak DNA-binding activity on its own (Chou et al., 1992; Griffith et al., 1992).Consistent with its role as a detector of DSBs, Ku binds linear DNA significantly better than closed supercoiled DNA (Blier et al., 1993).Similar to many other proteins involved in DNA metabolism (Hingorani and O'Donnell, 2000), Ku forms a toroid ...In 1994 the first human autoantigen (Ku protein) was identified as DNA helicase [25]. In 1996 Tuteja and his colleagues reported the first plant DNA helicase in the purified form from pea chloroplast [26] and Subramanya and his colleagues solved the crystal structure of the first DNA helicase (PcrA from thermophilic bacterium) [27].Sep 2, 2021 · The effect of MCL1 on DSBs goes beyond its effects on DDR protein foci accumulation. MCL1 binds and inhibits Ku, an essential NHEJ protein that stabilizes the DNA ends to promote ligation 54 (Fig ... Dynan, W. S. & Yoo, S. Interaction of Ku protein and DNA-dependent protein kinase catalytic subunit with ... References 103–107 identify RIF1 as a 53BP1 effector protein during DSB repair ...DNA-dependent protein kinase, catalytic subunit, also known as DNA-PKcs, is an enzyme that in humans is encoded by the gene designated as PRKDC or XRCC7. DNA-PKcs belongs to the phosphatidylinositol 3-kinase-related kinase protein family. The DNA-Pkcs protein is a serine/threonine protein kinase consisting of a single polypeptide chain of …Aravind, L. & Koonin, E.V. Prokaryotic homologs of the eukaryotic DNA-end-binding protein Ku, novel domains in the Ku protein and prediction of a prokaryotic double-strand break repair system.

(C) Electrophoretic mobility shift assay of radiolabeled ds DNA probe incubated with purified human recombinant Ku protein in the presence of various competitor ssO bearing a biotin moiety at the 3′-, 5′- or 3′- and 5′- end, blocked or not by streptavidin, as indicated. ds probe and ssO amount in reactions were 0.2 and 10 pmol ...Protein Purification. Native DNA-PKcs and Ku protein were purified from HeLa cell nuclear extracts as described previously, except that the phenyl-Superose and Mono S steps were omitted (35).To produce recombinant Ku protein, a 100-ml suspension culture of Sf9 cells was grown to a density of 1.5 × 10 6 cells/ml and was co-infected with VBB2-86Ku and VBB270tH 6 (36).Model for NHEJ. A IR induces DSBs, often with damaged ends that contain non-ligatable end groups (stars).B A Ku heterodimer (composed of Ku70, orange; Ku80, red) binds to each end of the DSB and C recruits DNA-PKcs (shown with head /kinase-FAT-FATC domain in pink and circular cradle in green) to form a synaptic complex.D The Ku complex also recruits a single homodimer of XLF (dark blue) that ...The Ku protein is localized in the nucleus and is composed of subunits referred to as Ku70 (p70) and Ku86 (p86) which is also known by the synonym Ku80 or (p80). Ku was first described as an autoantigen to which antibodies were produced in a patient with scleroderma polymyositis overlap syndrome, and was later found in the sera of patients with ...The Ku protein is a heterodimer composed of 70 kD (Ku70) and 80 kD (Ku80) subunits. Ku is the regulatory component of the DNA-dependent protein kinase (DNA-PK) that has a catalytic subunit of approximately 460 kD (DNA-PK(cs)). In this study, the two polypeptides (Ku80/Ku70) of the human Ku were expr …Here we show that the Saccharomyces cerevisiae palmitoyltransferase Pfa4 enhanced heterochromatin formation at the cryptic mating-type loci HMR and HML via Rif1, a telomere regulatory protein. Acylated Rif1 was detected in extracts from wild-type but not pfa4Δ mutant cells.Ku and DNA-dependent protein kinase dynamic conformations and assembly regulate DNA binding and the initial non-homologous end joining complex. J Biol Chem 2010; 285:1414-1423.Ku is a complex composed of two protein subunits of 70 and 80 kDa, hereafter designated as Ku70 and Ku80, respectively (1).It was shown that Ku is the DNA-binding component of a DNA-dependent protein kinase (DNA-PK) 1 that phosphorylates several nuclear proteins in vitro,e.g. p53, RNA polymerase II, or Ku itself and is involved in DNA double-strand break (DSB) repair and V(D)J recombination (2 ...

Identification of prokaryotic Ku homologs allowed the dissection of the Ku protein sequences into three distinct domains, the Ku core that is conserved in eukaryotes and prokaryotes, a derived von Willebrand A domain that is fused to the amino terminus of the core in eukaryotic Ku proteins, and the newly recognized helix–extension–helix ...

Protein is essential to good health. While not everyone needs to chug protein shakes and bars like bodybuilders, they do need to include it as part of their healthy diet. Learn why it’s important and how to calculate your daily protein need...Then the Ku heterodimer recruits to the DSB the catalytic subunit of DNA-dependent protein kinase DNA-PKcs (gene PRKDC). Altogether, Ku70, Ku80, and DNA-PKcs form a DNA-dependent protein kinase holoenzyme (DNA-PK), which protects and holds together two ends of the broken DNA, and serves as a scaffold for other proteins of the cNHEJ pathway (e.g ...Ku protein, a heterodimer of 70 and 83 kDa polypeptides, is the regulatory component of the DNA-dependent protein kinase (DNA-PK). Ku protein binds to DNA ends and is essential for DNA double-strand break repair and V(D)J recombination. Although there is some evidence that Ku protein also binds RNA, its RNA binding properties have not been systematically explored. In the present study, Ku ...First, Ku has been found associated with RNA polymerase II (Pol II) elongation sites 121, which is mediated by protein–protein interactions between …Although Ku80 requires Ku70 for binding to DNA, Ku70 may display some weak DNA-binding activity on its own (Chou et al., 1992; Griffith et al., 1992).Consistent with its role as a detector of DSBs, Ku binds linear DNA significantly better than closed supercoiled DNA (Blier et al., 1993).Similar to many other proteins involved in DNA metabolism (Hingorani and O'Donnell, 2000), Ku forms a toroid ...Unexpectedly, we found that abolishing Ku protein gene function perturbs mating type determination and generates selfing clones in Tetrahymena. Detailed analysis uncovers unusual DNA rearrangement steps in Tetrahymena mating type determination, sheds light on the molecular nature of self-nonself-discrimination, and reveals an unexpected phase ...Given that Ku70/Ku86 heterodimer is a DNA binding protein that is mainly localized in the nuclei of cells (Walker et al., 2001; Fell and Schild-Poulter, 2015), our findings suggest that Ku protein is mislocalized in DAOY cells, indicating that DAOY cells carry a Ku malfunction in regards to their nuclear functions in DNA repair and telomere ...© STRING Consortium 2023. SIB - Swiss Institute of Bioinformatics; CPR - Novo Nordisk Foundation Center Protein Research; EMBL - European Molecular Biology LaboratoryThe repair of DNA double-strand breaks (DSBs) is critical for the maintenance of genomic integrity and viability for all organisms. Mammals have evolved at least two genetically discrete ways to mediate DNA DSB repair: homologous recombination (HR) and non-homologous end joining (NHEJ). In mammalian …

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Model for NHEJ. A IR induces DSBs, often with damaged ends that contain non-ligatable end groups (stars).B A Ku heterodimer (composed of Ku70, orange; Ku80, red) binds to each end of the DSB and C recruits DNA-PKcs (shown with head /kinase-FAT-FATC domain in pink and circular cradle in green) to form a synaptic complex.D The Ku complex also recruits a single homodimer of XLF (dark blue) that ...The DNA-dependent protein kinase (DNA-PK) is a serine/threonine protein kinase composed of a large catalytic subunit (DNA-PKcs) and the Ku70/80 heterodimer. Over the past two decades, significant progress has been made in elucidating the role of DNA-PK in non-homologous end joining (NHEJ), the major pathway for repair of ionizing radiation-induced DNA double strand breaks in human cells and ...Masagipedia.com - Berikut adalah contoh RKH atau RPPH Kurikulum Merdeka PAUD dan TK semester 1 Tema Kebutuhanku dengan Sub Tema Makanan pertemuan ke 6.. RPPH Kurikulum Merdeka Belajar PAUD dan TK ini bisa dijadikan referensi guru dalam pembuatan rencana pembelajaran harian di satuan pendidikan …Strikingly, loss of KU fully rescued the anemia in DNA-PKcs 5A/5A mice, suggesting a cNHEJ independent function of DNA-PKcs in erythrocyte differentiation and protein translation. In this context, we and others found that KU as well as DNA-PKcs gather in nucleoli in a detergent resistant manner independent of other cNHEJ factors [ 86 , 187 ].We would like to show you a description here but the site won’t allow us.DNA-dependent protein kinase catalytic subunit (DNA-PKcs) has a high affinity for Ku-DNA ends and, together with Ku, forms the DNA-PK complex 4 . Figure 1: Overview of non-homologous end joining.Function. 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 .The dissection of the Ku protein from eukaryotes and prokaryotes into individual domains described above suggests an evolutionary scenario for these proteins. The Ku core is an ancient domain that was probably present in bacteria and archea even before the advent of the eukaryotes. There are clear indications that, in these organisms, the Ku ...Ku proteins promote DNA binding and condensation of cyclic GMP-AMP synthase. Xinyue Tao 1 3 4 5. , Jiali Song 2 5. , Ying Song 2. , Yao Zhang 2. , Jing Yang … ….

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 the completion ...The DNA-dependent protein kinase (DNA-PK), which comprises the KU heterodimer and a catalytic subunit (DNA-PKcs), is a classical non-homologous end-joining (cNHEJ) factor1. KU binds to DNA ends ...Human Ku heterodimeric protein composed of Ku70 and Ku80 subunits plays an important role in the non-homologous end-joining DNA repair pathway as a sensor of double strand DNA breaks. Ku is also involved in numerous cellular processes, and in some of them it acts in an RNA-dependent manner. However, …Structurally, the Ku protein forms an expansive base and a very narrow bridge, producing a toroidal structure that allows Ku to slide onto the ends of DSBs (14, 37). Furthermore, Ku has oriented DNA binding and along with its unique toroidal dsDNA binding region results in tight and sustained binding to DNA ends limiting the ability for Ku to ...Article Ku proteins promote DNA binding and condensation of cyclic GMP-AMP synthase Xinyue Tao,1,3,4,5 Jiali Song,2,5 YingSong,2 Yao Zhang,2 JingYang,1,3 Pengfei Zhang,1,3 DechongZhang,2 Dahua ...Telomere length maintenance, an activity essential for chromosome stability and genome integrity, is regulated by telomerase- and telomere-associated factors. The DNA repair protein Ku (a heterodimer of Ku70 and Ku80 subunits) associates with mammalian telomeres and contributes to telomere maintenance. Here, we analyzed the physical association of Ku with human telomerase both in vivo and in ...The Ku heterodimer is a well conserved protein(s), with homologs known to exist in every species from bacteria to humans . In all organisms examined, mutations in either Ku subunit result in the expected deficits in DNA DSB repair, DNA recombination, and sensitivities to DNA-damaging agents. Importantly, in all organisms, with one glaring ... Ku protein, [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1], [text-1-1]