Ku protein
Ku, a heterodimer of Ku70 and Ku80, plays a key role in multiple nuclear processes, e.g. DNA repair, chromosome maintenance, and transcription regulation. Heterodimerization is essential for Ku-dependent DNA repairin vivo, although its role is poorly understood. Some lines of evidence suggest that heterodimerization is required for the stabilization of Ku70 and Ku80.Jun 24, 2023 · The nuclear pore complex is the key regulator of transport between the cytoplasm and nucleus. Emerging evidence suggests it also regulates gene expression by influencing the internal architecture ...The mixture was excited at 435 nm, and emission was recorded between 440 and 650 nm. One microgram of ECFP-Ku70/EYFP-Ku80 (or a Ku mutant protein) was incubated for 60 minutes in 80 µL FRET buffer (25 mM Tris-HCl pH8.0, 120 mM KCl, 10 mM MgCl 2, and 2 mM DTT). DNA oligonucleotide substrates were prepared in FRET buffer containing 2 μg ...
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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.Mar 27, 2021 · In yeast, KU protein slides onto the DNA end and translocates inward. Ku interacts with the DNA ligase IV complex. The catalytic subunit of DNA ligase IV, along with its co-factors Dnl4 and Lif1, performs the DNA repair. Recent studies suggest that in yeast, the Nej1, which is homologous to mammalian XLF, may promote re-adenylation of DNA ...Addition of Ku protein stimulates the kinase activity 5 - 10-fold (Yaneva et al., 1997). Based on the abundant amount of Ku in cells, it is likely that activation of DNA-PK by DSBs in vivo ...Prof. Anja Groth leads a research group at the the Novo Nordisk Foundation Center for Protein Research (CPR), Faculty of Health and Medical Sciences, University of Copenhagen. Anja Groth received her PhD in Molecular Biology from the University of Copenhagen in 2004 for her research in the laboratory of Drs. Lukas and Bartek.Eight sera contained isolated antibodies to Ku proteins: both subunits were recognized in 7 cases, while isolate reactivity to the 70 kDa protein was detected in one case. Five sera contained additional antibody specificities: anti-Ro 60 kDa in 4 cases, and anti-La/SSB, anti-SL, and anti-PM-Scl in one case each.Collectively, our data show that zinc-finger protein ZNF384 is an adapter of Ku to DNA during DSB repair via cNHEJ. Results. ZNF384 is recruited to DNA damage sites and interacts with NHEJ proteins.Matthias Mann is Research Director and Group leader at the Proteomics Program at Novo Nordisk Foundation Center for Protein Research (CPR, www.cpr.ku.dk) at the University of Copenhagen. He also holds a Director position at the Max-Planck Institute of Biochemistry in Munich. Matthias Mann is one of the most highly cited researchers in the world ...We have shown that the Ku protein, an autoantigen, or an inhibitor associated with this protein can suppress RNA polymerase I (Pol I) transcription of the rat ribosomal RNA gene when the cells are starved for serum , although Ku is a positively acting Pol I transcription factor under normal growth conditions (23, 24). The present study was ...They form heterodimeric complex known as KU protein and bind to DNA-PK (DNA-dependent protein kinase) to create active holoenzyme. Active DNA-PK complex mediates the DSBs repair through NHEJ. Additionally DNA-PK can phosphorylate Thr5 and Thr7 residues of chaperone protein HSP90 (heat shock protein 90) subunit alpha, which is responsible for ...Fig. 1 shows that in this assay Ku protein led to the retention of the [32P]DNA probe in a concentration-dependent manner. It can be seen that Ku binds double-stranded DNA more readily than single-stranded DNA. At maximal binding, 40 fmol of Ku protein are capable of binding 90% of the double- stranded DNA probe (25 fmol) used in the assay. The ...4. I am looking to purchase Pyruvate Kinase from the Sigma Website, they state the volume in Kilo Units (KU) i.e. 1, 5 or 25 KU. It also states there are 350-600 units / mg protein. …Furthermore, the Ku protein plays essential roles in protecting DSB against resection and in promoting subtelomeric gene repression (Boulton and Jackson 1996, 1998). More recently, artificially tethering the ATM checkpoint kinase Tel1 or the DNA repair protein Mre11 to a defective silencer was shown to promote silencing at this locus.In most cells, Ku (an heterodimer of two tightly associated sub-units called Ku70 and. Ku80), is an abondant protein located in the nucleus, where it plays a ...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). The Ku heterodimer (Ku70/Ku80) plays a central role in DNA double strand break recognition and repair. It has been shown, more than ten years ago, that Ku is also expressed at the cell surface of different cells types along with its intracellular pool within the nucleus and the cytoplasm but involvement of Ku in cell-cell and cell-extracellular matrix adhesion has been only recently demonstrated.Ku70 (IPR006165) and Ku80 (IPR024193) share three domains: Ku N-terminal α/β (IPR005161), Ku70/Ku80 β-barrel (IPR006164), and Ku helical C-terminal (IPR005160). Ku70 and Ku80 have divergent C-terminal regions. ... Prokaryotic homologs of the eukaryotic DNA-end-binding protein Ku, novel domains in the Ku protein and prediction of a ...
The DNA-dependent protein kinase: requirement for DNA ends and association with Ku antigen. Cell 72 , 131-142 (1993). Article CAS PubMed Google ScholarJun 18, 2023 · Nature子刊：中山大学松阳洲团队发现DNA损伤修复通路的新选择. DNA双链断裂 （DNA double-strand break，DSB）是一种常见且高度有害的DNA损伤形式，严重威胁着基因组稳定性和细胞存活。. DSB修复缺陷或失调与肿瘤、衰老以及免疫缺陷等密切相关。. 非同源末端连接（Non ...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.Coilin is a nuclear protein that plays a role in Cajal body formation. The function of nucleoplasmic coilin is unknown. Here we report that coilin interacts with Ku70 and Ku80, which are major players in the DNA repair process. Ku proteins compete with SMN and SmB′ proteins for coilin interaction sites.In this study, we have examined the involvement of Ku in breast tumorigenesis and tumor progression and found that the Ku protein expression levels in human breast metastatic (MCF10AC1a) cells were higher in the chromatin fraction compared to hyperplastic (MCF10AT) and normal (MCF10A) human breast cells, but remained constant in both the ...
Nomenclature Ku80 has been referred to by several names including: Lupus Ku autoantigen protein p80 ATP-dependent DNA helicase 2 subunit 2 X-ray repair complementing defective repair in Chinese hamster cells 5 X-ray repair cross-complementing 5 (XRCC5) Epigenetic repression 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 ...…
Reader Q&A - also see RECOMMENDED ARTICLES & FAQs. Overview The Ku proteinor X-ray repair cross-c. Possible cause: Start GRAMM docking. We are looking for Postdocs and PhD students, prefera.
Therefore, Ku protein neddylation is associated with Ku protein ubiquitination, which may induce apoptotic cell death. Astaxanthin, an oxygen-containing carotenoid (xanthophyll), is present in marineThe Artemis protein and the Xrcc4/DNA ligase IV heterodimer are then recruited, with Artemis involved in the maturation of the DSB ends and the Xrcc4/DNA ligase IV complex catalysing the re-sealing of the ends [12], [13]. The KU heterodimer is composed of 70–86 kDa subunits, respectively called Ku70 and Ku80 (or Ku86) [14].
The GRAMM-X Protein Docking Web Server has been discontinued. The new GRAMM Docking Web Server can be found at ...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 ...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]
The Ku heterodimer, consisting of two subunits, Ku70 an DNA-PK is a nuclear serine/threonine protein kinase comprising a DNA-binding subunit, the Ku autoantigen, and a large catalytic subunit (460 kDa), DNA-PKcs. The Ku autoantigen is a heterodimer of the Ku70 and Ku80 proteins that binds to DNA double-strand ends and recruits DNA-PKcs [ 23 – 25 ]. Ku protein mainly functions in the cell in themultifunctional ATP-dependent Ligase-D and Ku protein that We propose that 5’ adenosine monophosphate-activated protein kinase (AMPK) ... Kim YN, Kim HS, Kim HT, Park JY, Lee KU, Jang WG, Kim JG, Kim BW, Lee IK. Effects of PGC-1alpha on TNF-alpha-induced MCP-1 and VCAM-1 expression and NF-kappaB activation in human aortic smooth muscle and endothelial cells.The F-box protein Fbxl12 binds to DSBs in a Ku-sensitive manner. (A) 35 S-labeled Xenopus tropicalis Fbxl12 and histone H3 were added to egg extract that was either mock- or Ku-depleted. Streptavidin-coated (SA), SB-DNA, or DB-DNA beads were added to the mock-depleted extract and SB-DNA beads were added to the Ku-depleted extract. As Ku protein has been extensively studied DNA-PKcs pushes Ku protein inwards onto the DNA, and then phosphorylates the other components nearby, including its own phosphorylation. DNA-PKcs autophosphorylation can be regulated by N-terminal conformational changes of protein (Meek et al., 2012). In addition to the automatic regulation of DNA-PKcs, many other factors are also suggested to ... The Ku protein binds to DNA ends and other types of discontiThe DNA-dependent protein kinase (DNA-PK), which comprises tMatthias Mann is Research Director and Grou INTRODUCTION. The Ku protein, a heterodimer consisting of Ku70 and Ku80 subunits, is a multifunctional complex playing critical roles in important cellular processes such as non-homologous end joining (NHEJ), V(D)J recombination, apoptosis, telomere maintenance and DNA replication ().The most well-studied function of Ku is its DNA-PKcs dependent role in NHEJ pathway, where it functions as a ... Start GRAMM docking. We are looking for Postdocs and PhD studen The pattern of Ku protein cross-linking in Figure 6D and E is remarkably similar to the results obtained in an earlier study characterizing the binding of Ku protein to a 14mer probe . To facilitate comparison, the results of the earlier work are summarized here in Figure 6F and G. With both the 14mer and the 28mer probes, Ku70 formed strong ... We explore unique structural and functional aspects, detai[We explore unique structural and functional aspects, detail KThe Mt-Ku fusion protein was over-expressed i Ku, another protein required for NHEJ, also stimulates LX ligation non-specifically and enhances DNA bridging [17]. Indeed, there is a striking similarity between Ku and AHNAK in this context since Ku also interacts with LX on the DNA molecule and, based on a specific interaction with LX, has been suggested to recruit LX to DNA [53] .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.