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Polθ is phosphorylated by PLK1 to repair double-strand breaks in mitosis

DNA double-strand breaks (DSBs) are deleterious lesions that challenge genome integrity. To mitigate this threat, human cells rely on the activity of multiple DNA repair machineries that are tightly regulated throughout the cell cycle1. In interphase, DSBs are mainly repaired by non-homologous end joining and homologous recombination2. However, these pathways are completely inhibited in mitosis3–5, leaving the fate of mitotic DSBs unknown. Here we show that DNA polymerase theta6 (Polθ) repairs mitotic DSBs and thereby maintains genome integrity. In contrast to other DSB repair factors, Polθ function is activated in mitosis upon phosphorylation by Polo-like kinase 1 (PLK1). Phosphorylated Polθ is recruited by a direct interaction with the BRCA1 C-terminal domains of TOPBP1 to mitotic DSBs, where it mediates joining of broken DNA ends. Loss of Polθ leads to defective repair of mitotic DSBs, resulting in a loss of genome integrity. This is further exacerbated in ....

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From Protein Design to the Energy Landscape of a Cold Unfolding Protein

From Protein Design to the Energy Landscape of a Cold Unfolding Protein
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Hydrophilic Forces In Protein Folding , Relaxation Dispersion Nuclear Magnetic Resonance Spectroscopy , Bond Network , Network Of More , O Statistical Survey Of The Buried Waters , Dp Cooperative Cold Denaturation , Hydrodynamic Properties Of The Cold Denatured , Temperature Properties Of Human , D On The Cooperative Formation Of Non , Mh Cooperative Thermal Denaturation Of Proteins , Nucleic Acid Hydrodynamic Properties , View Of Hydrophobic Free Energy , Stanford Synchrotron Radiation Laboratory , J Cooperative Protein , Modular Hydrogen , M Limited Cooperativity , Ka Dominant Forces In Protein Folding , Magnetic Resonance Data Bank , Energy Landscape Of The Protein Isc , Jb How Cooperative Are Protein Folding , Equilibrium Free Energy Relationships , Protein Data Bank , A Transfer Free Energy , Dominant Forces , Protein Structure Prediction , Protein Folding Problem ,

NMR Spectroscopy Principles, Interpreting an NMR Spectrum and Common Problems

Nuclear magnetic resonance (NMR) spectroscopy is a physicochemical technique used to obtain structural information about molecules. In this article, we consider how it works, what it tells you and where it is used. ....

New York , United States , Felix Bloch , Olugbengae Abimbola , Vlaardingerbroek Mt Boer , Pharmaceut Biomed , Friebolinh Becconsall , Edwardm Purcell , Du Vernetr Boekelheidev Nuclear , Nuclear Overhauser , Nuclear Overhauser Effect Spectroscop , Magnetic Resonance Data Bank , Hatzakise Nuclear , Harvard University , Oxford University Press , Packardm Nuclear , Oxford University , Stanford University , Nuclear Magnetic Resonance In Modern Technology , Nobel Prize , Biological Magnetic Resonance Data Bank , Spectral Database , Organic Compounds , Correlated Spectroscopy , Nuclear Overhauser Effect Spectroscopy , Nucl Mag Res ,

NSF award to establish network for advanced NMR across three institutions

NSF award to establish network for advanced NMR across three institutions
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University Of Georgia , United States , Jeff Hoch , John Markley , Robin Davies , Katie Henzler Wildman , Magnetic Resonance Data Bank , National Science Foundation , Network For Advanced , University Of Wisconsin , Madison National Magnetic Resonance Facility At , Uconn School Of Medicine , Chad Rienstra , National Magnetic Resonance Facility , Structural Biology , Art Edison , Biological Magnetic Resonance Data Bank , பல்கலைக்கழகம் ஆஃப் ஜார்ஜியா , ஒன்றுபட்டது மாநிலங்களில் , ஜெஃப் ஹாக் , ஜான் மார்க்லி , ராபின் டேவிஸ் , காந்த அதிர்வு தகவல்கள் வங்கி , தேசிய அறிவியல் அடித்தளம் , பல்கலைக்கழகம் ஆஃப் விஸ்கான்சின் , உக்கொண்ங் பள்ளி ஆஃப் மருந்து ,