Ku protein

If peanut IgE is 0.10 kU/L or greater, then 7 peanut components (Ara h 2, Ara h 1, Ara h 3, Ara h 6, Ara h 8, Ara h 9, and profilin Bet v2) are performed at an additional charge. ... Group 1 Fagales-related protein (h 8) PR-10 Protein (h 8) Non-specific Lipid Transfer Protein (ns-LTP) (h 9) PR-14 Protein (h 9) Bet v2. Profilin.

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 ...Mar 7, 2021 · Ku70 and Ku80 form a heterodimer called Ku protein, which is well known for its role in repairing DNA double‐strand breaks by non‐homologous end joining (NHEJ). 33 So, we are curious about the localization of Ku80, while Ku70 undergoes a translocation from the nucleus to the cytoplasm. Ara h 3. • Sensitization to Ara h 1, 2 and 3 is usually acquired in childhood. 16. • IgE to Ara h 2 has the best discriminative ability of all diagnostic tests for peanut allergy. It can accurately diagnose peanut allergy in 28% of patients but cannot be used to exclude a peanut allergy in an adult population. 6,12-16.Ku70 and Ku80 form a heterodimer, Ku, which possesses DNA end-binding activity (Mimori and Hardin, 1986). 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).Non-homologous end joining proteins and their known interactions. a | The non-homologous end joining (NHEJ) DNA protein kinase (DNA-PK) complex consists of a heterodimer of Ku70 and Ku80 plus DNA-PK catalytic subunit (DNA-PKcs). Ku70 and Ku80 consist of von Willebrand (vWA) domains, the Ku core and the nuclear localization sequence (NLS).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.We'd like to inform you that we have updated our Privacy Notice to comply with Europe's new General Data Protection Regulation (GDPR) that applies since 25 May 2018 ...

The design of potent inhibitors of Ku-DNA or Ku-protein interactions will be central to characterize new molecules that may serve as a radiosensitizer or to improve genome editing. Acknowledgments. We would like to thank Patrick Calsou (IPBS, Toulouse), Stephane Marcand and Florian Roisné-Hamelin (Institut Jacob, iRCM, Fontenay aux rose), and ...Ku proteins are present in subcellular structures other than the nucleus. For example, Ku70 has been shown to bind to the pro-apoptotic complex and inhibit BAX …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 ...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)).Start GRAMM docking. We are looking for Postdocs and PhD students, preferably with physics/math background, to work on modeling of protein interactions and whole cell modeling. Letters of interest and CVs can be sent to [email protected]. Email Address: PDB file of the receptor: ⓘ. PDB file of the ligand: ⓘ. Docking methodology: ⓘ. Number of ...Ku is an ubiquitous nuclear heterodimeric protein consisting of p70 and p86 subunits that binds double-stranded DNA termini and associates with chromosomes in vivo. It was originally described as an autoantigen in patients with certain autoimmune diseases. The individual subunits of Ku have been difficult to isolate from human cells without ...

The key factors of NHEJ are a Ku protein that binds to the termini of the double-strand breaks and has the bridging activity, and a ligase that ligates the termini. Our results indicate that NHEJ genes are present in few bacteria (Ku is present in 24 genomes out of the 117), with no particular phylogenetic trend, as they are found in firmicutes ...Ku adopts ring shaped structure and acts as a DNA targeting subunit of the DNA-dependent protein kinase catalytic subunit (DNA PKcs or XRCC7) which along with Ku forms DNA-PK holoenzyme. DNA-PKcs induce an inward translocation of Ku protein allowing DNA-PKcs to contact opposing DSB ends.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 Ku protein complex is involved in length regulation of Drosophila telomeres. Genetics 170 , 221-235 (2005). Article CAS PubMed PubMed Central Google ScholarFunction. 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 .

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Earlier, we have reported that 70 kDa subunit of Ku protein heterodimer (Ku70) binds and inhibits Bax activity in the cytosol and that ubiquitin (Ub)-dependent proteolysis of cytosolic Ku70 ...We would like to show you a description here but the site won’t allow us.The DNA end-binding protein Ku protein plays an important role in mammalian NHEJ. Owing to its ring-shaped structure, Ku threads onto exposed DNA termini (Fig. 1A).Following DNA binding by Ku, DNA-PK is assembled and the DNA Ligase IV complex is recruited to the site of the break (Fig. 1C).Highlighting the central role of Ku in NHEJ, deficiencies in Ku have been shown to result in defects in ...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 …

When Ku protein was fractionated electrophoretically, transferred to nitrocellulose filter, and probed with 32P-labeled DNA, only the 70,000-dalton subunit exhibited DNA binding. Thus, the Ku protein appears to recognize selectively ends of double-stranded DNA molecules. Possible functions of the Ku autoantigen in eukaryotic cells are discussed.The Ku (p70/p80) autoantigen, a heterodimer consisting of 70 kDa (p70) and 80 kDa (p80) protein subunits, is one of a group of DNA-associated autoantigens identified as targets of autoantibodies produced by patients with SLE and related disorders. Many of these DNA-protein antigens are involved in organizing the genome into transcriptionally ...Protein-ligand (PL) interactions have drawn great amounts of scientific attention throughout the last century (see refs. 1,2,3,4. for a few recent textbooks and reviews).Aside from being examined ...Anderson C (1993) DNA damage and the DNA-activated protein kinase. Trends Biochem Sci 18:433–437. CrossRef PubMed CAS Google Scholar . Beall E, Admon A, Rio D (1994) A Drosophila protein homologous to the human p70 Ku autoimmune antigen interacts with the P transposable element inverted repeats. Proc Natl Acad Sci USA 91:12681–12685Ku 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). Eukaryotic Ku is a heterodimer of two polypeptides, Ku70 (XRCC6) and Ku80 (XRCC5), so ...The invention provides an application of mycobacterium Ku protein. The invention provides a new mark, belongs to ku gene/protein of NHEJ system, and can be used for identification of mycobacteria and differential identification of MTBC and NTM in the mycobacteria. The prevalence of the ku gene in mycobacteria and the rarity of prokaryotic cells determine the applicability and high specificity ...9 Agu 2001 ... The Ku heterodimer, consisting of two subunits, Ku70 and Ku80, is a member of a family of DNA repair proteins that fixes damaged DNA in order to ...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 ... Ku is a dimeric protein complex that binds to DNA double-strand break ends and is required for the non-homologous end joining pathway of DNA repair. Ku is …Identified in a complex with DEAF1 and XRCC5 ( PubMed: 22442688 ). Interacts with DEAF1 (via the SAND domain); the interaction is direct and may be inhibited by DNA-binding ( PubMed: 22442688 ). Interacts with CLU ( By similarity ). Interacts with NR4A3; the DNA-dependent protein kinase complex DNA-PK phosphorylates and activates NR4A3 and ...Moving down the Ku protein, the Ku extended C-terminal region from both B. subtilis and Mycobacterium smegmatis, permits binding to supercoiled DNA (13, 24). This extended C-terminal region also limits translocation on linear dsDNA for B. subtilis Ku and plays a role in stimulating ligation (12, 13). How do these functions compare to Ku ...

Advances in massively parallel sequencing, of complete bacterial genomes, have led to many novel findings in the field of genomics. However, these data often lack correlation with expressed protein profiles. It has been demonstrated that even very closely related genomes, such as in mycobacteria, express drastically different phenotypes. …

The Ku protein (Ku70-Ku80) is involved in various genome-maintenance processes such as DNA replication and repair, telomere maintenance, and chromosomal stability. We previously found that Ku80 is implicated in the loading of members of the pre-replicative complex (pre-RC) onto replication origins. …Interactions of Ku protein with DNA duplexes are characterized by high affinity, whereas its affinity to single-stranded DNA is by several orders of magnitude lower [15]. The structural basis for the predominant recognition of the duplex DNA ends by Ku is demonstrated in the crystal structure of human Ku bound to DNA [16]. The two Ku subunits ...Oct 14, 2021 · The Ku protein also has a high affinity to DNA due to its form being preset for the helix. As a result of the asymmetric ring, there is a strong preference (Kd value of 1.5 to 4 X 10^-10 M) for the Ku ring to slide onto the ends of DNA . In addition, other asymmetric features, such as a abundance of Asp residues on the N terminus of the Ku Ring ... Introduction. Ku protein is an important component of the nonhomologous end‐joining (NHEJ) pathway of DNA double‐strand break repair, and it is ubiquitous among eukaryotes. 1-5 Some bacterial species encode a homolog of Ku, and bacterial Ku proteins function along with a dedicated ligase to repair DNA double‐strand breaks and protect against genome rearrangements (for review, see Ref. 6).Identified in a complex with DEAF1 and XRCC5 ( PubMed: 22442688 ). Interacts with DEAF1 (via the SAND domain); the interaction is direct and may be inhibited by DNA-binding ( PubMed: 22442688 ). Interacts with CLU ( By similarity ). Interacts with NR4A3; the DNA-dependent protein kinase complex DNA-PK phosphorylates and activates NR4A3 and ...Oct 14, 2023 · the Ku protein, which is present in many bacteria such as Actinomycetes, Bacillus, Agrobacterium and Methanosar-cina [7–13], generally binds to DSBs but does not inter-act with closed circular DNA because it first recognizes DNA ends and then transfers them to internal sites [14]. The LigD protein, an ATP-dependent ligase also found inAug 5, 1986 · When Ku protein was fractionated electrophoretically, transferred to nitrocellulose filter, and probed with 32P-labeled DNA, only the 70,000-dalton subunit exhibited DNA binding. Thus, the Ku protein appears to recognize selectively ends of double-stranded DNA molecules. Possible functions of the Ku autoantigen in eukaryotic cells are discussed. Ku protein binds to DNA ends and is a cofactor for the DNA-dependent protein kinase. Both of these components are involved in DNA double-strand break repair, but it has not been clear if they function indirectly, by sensing DNA damage and activating other factors, or if they are more directly involved in the processing and rejoining of DNA breaks.

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DNA looping by Ku and the DNA-dependent protein kinase. Proc Natl Acad Sci U S A 94, 4267–4272. [PMC free article] [Google Scholar] Chan DW, and Lees-Miller SP (1996). The DNA-dependent protein kinase is inactivated by autophosphorylation of the catalytic subunit. J Biol Chem 271, 8936–8941. [Google Scholar]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 …Through protein-protein contacts eventually reinforced by protein-DNA interactions, the Ku-DNA hub attracts a series of specialized proteins with scaffolding and/or enzymatic properties. To shed light on these dynamic interplays, we review here current knowledge on proteins directly interacting with Ku and on the contact points involved, with a ...Protein is a nutrient your body needs to grow and repair cells, and to work properly. Protein is found in a wide range of food and it’s important that you get enough protein in your diet every day. How much protein you need from your diet varies depending on your weight, gender, age and health. Meeting your protein needs is easily achieved ...Bacterial Ku is usually found as a single gene and exists as homodimers. It is much smaller than the eukaryotic Ku proteins and does not include the vWA and SAP domains that make Ku 70/80 distinct. These additional domains allow eukaryotic Ku to behave as a scaffold protein and interact with the variety of factors in the more complex NHEJ system. High blood protein is not usually accompanied by symptoms and is usually diagnosed through a blood test, according to Mayo Clinic. While it is not a disorder, high blood protein can sometimes indicate the presence of a disease.The Ku protein consists of two tightly associated homologous subunits, Ku70 and Ku80, and was originally identified as an autoantigen recognized by the sera of patients with an autoimmunity disease. In eukaryotes, the Ku heterodimer contributes to genomic integrity through its ability to bind DNA double-strand breaks and facilitate repair by ...Ku protein mainly functions in the cell in the form of a very stable heterodimer . However, some research demonstrates that isolated Ku70 and Ku80 subunits can be involved in certain processes . The Ku70/Ku80 heterodimer is a DNA-binding protein that mostly interacts with the free ends of doublestranded DNA, and its biological function is ...Oxidative stress induces DNA damage which can be repaired by DNA repair proteins, such as Ku70/80. Excess reactive oxygen species (ROS) stimulate the activation of caspase-3, which degrades Ku 70/80. Cells with decreased Ku protein levels undergo apoptosis. Astaxanthin exerts antioxidant activity by inducing the expression of catalase, an antioxidant enzyme, in gastric epithelial cells ...The eukaryotic Ku protein has key roles in DNA repair and in certain transposition events. Here we show that the Gam protein of phage Mu is conserved in bacteria, has sequence homology with both subunits of Ku, and has the potential to adopt a similar architecture to the core DNA-binding region of Ku.The Ku protein, a DNA-binding complex that is composed of two subunits of 70 kDa and of 86 kDa, has been suggested to play a role in gene transcription. The dependence of the in vitro DNA-binding activity of affinity-purified Ku protein on reduced cysteine residues has been studied using sulphydryl-modifying agents.Biography —. Dr. Scott Lovell has served as Director of the Protein Structure Laboratory (PSXL) at the University of Kansas (KU) since 2008 and has 27 years of experience in the X-ray crystallography field. He received his Ph.D. from Purdue University in chemistry where he was trained in X-ray crystallography and studied the structural and ... ….

The high affinity DNA binding factor (HDF) protein of Saccharomyces cerevisiae is composed of two subunits and specifically binds ends of double-stranded DNA. The 70-kDa subunit, HDF1, shows significant homology with the 70-kDa subunit of the human Ku protein. Like the Ku protein, HDF1 has been show …Ku protein and the DNA-dependent protein kinase catalytic subunit (DNA-PKcs) are essential components of the double-strand break repair machinery in higher eukaryotic cells. Ku protein binds to broken DNA ends and recruits DNA-PKcs to form an enzymatically active complex. To characterize the arrangement of proteins in this complex, we developed ...In contrast, PHR 2 and 3 ( Gell and Jackson 1999) map to the amino-terminal region exclusively shared by the eukaryotic Ku proteins. This core domain shared by the prokaryotic YkoV-like proteins and the eukaryotic Ku70 and Ku80 (hereinafter Ku core; Fig. 2) is ~234-280 amino acids long and is larger than most common globular domains.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 ...About this page Nonhomologous End Joining in Bacteria E.J. Bartlett, A.J. Doherty, in Encyclopedia of Biological Chemistry (Second Edition), 2013 Bacterial Ku All Ku proteins form dimeric ring-like structures, capable of sliding over DNA ends. Ku does not bind to specific genetic sequences, nor make extensive contacts with the phosphate backbone.Key Points Ku is a heterodimer composed of two subunits — Ku70 and Ku80 — that binds to DNA ends in a sequence-independent manner. Ku is found throughout eukaryotic evolution and in higher eukaryotes is associated with the DNA-dependent protein kinase... In all systems studied, Ku has been shown to ...The Ku-DNA complex is then recognized by the DNA-dependent protein kinase (DNA-PK) catalytic subunit (DNA-PKcs), with the ensuing DNA-Ku-DNA-PKcs complex forming the active DNA-PK serine/threonine kinase (Dvir et al., 1993; Gottlieb and Jackson, 1993). Finally, DSB ligation is mediated by the DNA ligase IV-XRCC4-XLF complex.Ku protein is a relatively abundant DNA-binding protein which was first detected as the autoantigen in a patient with scleroderma-polymyositis overlap syndrome (hence the name 'Ku'). It is a heterodimer of two polypeptide chains of molecular weights 85,000 and 72,000, and it characteristically binds, in vitro, to the ends of DNA fragments, and ...The heterodimeric Ku protein, which comprises a 86 kDa (Ku86) amd a 70 kDa (Ku70) subunits, is an abundant nuclear DNA-binding protein which binds in vitro to DNA termini without sequence specificity.The Ku heterodimer, composed of Ku70 and Ku80, is best characterized for its role in repairing double-stranded DNA breaks but is also known to participate in other regulatory processes. Despite our understanding of Ku protein interplay during DNA repair, the extent of Ku's protein interactions in other processes has never been fully determined. 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]