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2 results on '"Kay, Lewis E."'

1. In support of the BMRB

Author

Markley, John L, Akutsu, Hideo, Asakura, Tetsuo, Baldus, Marc, Boelens, Rolf, Bonvin, Alexandre, Kaptein, R, Bax, A., Bezsonova, Irina, Gryk, Michael R, Hoch, Jeffrey C, Korzhnev, Dmitry M, Maciejewski, Mark W, Case, Dave, Chazin, Walter J, Cross, Timothy A, Dames, Sonja, Kessler, Horst, Lange, Oliver, Madl, Tobias, Reif, Bernd, Sattler, Michael, Eliezer, David, Fersht, Alan, Forman-Kay, Julie, Kay, Lewis E, Fraser, James, Gross, John, Kortemme, Tanja, Sali, Andrej, Fujiwara, Toshimichi, Gardner, Kevin, Luo, Xuelian, Rizo-Rey, Jose, Rosen, Michael, Gil, Roberto R, Ho, Chien, Rule, Gordon, Gronenborn, Angela M, Ishima, Rieko, Klein-Seetharaman, Judith, Tang, Pei, van der Wel, Patrick, Xu, Yan, Grzesiek, Stephan, Hiller, Sebastian, Seelig, Joachim, Laue, Ernest D, Mott, Helen, Nietlispach, Daniel, Barsukov, Igor, Lian, Lu-Yun, Middleton, David, Blumenschein, Tharin, Moore, Geoffrey, Campbell, Iain, Schnell, Jason, Vakonakis, Ioannis John, Watts, Anthony, Conte, Maria R, Mason, James, Pfuhl, Mark, Sanderson, Mark R, Craven, Jeremy, Williamson, Michael, Dominguez, Cyril, Roberts, Gordon, Günther, Ulrich, Overduin, Michael, Werner, Joern, Williamson, Philip, Blindauer, Claudia, Crump, Matthew, Driscoll, Paul, Frenkiel, Tom, Golovanov, Alexander, Matthews, Steve, Parkinson, John, Uhrin, Dusan, Williams, Mark, Neuhaus, David, Oschkinat, Hartmut, Ramos, Andres, Shaw, David E, Steinbeck, Christoph, Vendruscolo, Michele, Vuister, Geerten W, Walters, Kylie J, Weinstein, Harel, Wüthrich, Kurt, Yokoyama, Shigeyuki, NMR Spectroscopy, Sub NMR Spectroscopy, NMR Spectroscopy, and Sub NMR Spectroscopy

Subjects
MEDLINE, Nanotechnology, Fund Raising, Biology, chemistry, protein database, Financial management, 03 medical and health sciences, Structural Biology, Taverne, Animals, Humans, Fund raising, animal, human, Databases, Protein, Molecular Biology, Nuclear Magnetic Resonance, Biomolecular, 030304 developmental biology, 0303 health sciences, business.industry, 030302 biochemistry & molecular biology, article, Protein database, Proteins, economics, financial management, Data science, nuclear magnetic resonance, business, protein
Published
2012
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2. The RNF168 paralog RNF169 defines a new class of ubiquitylated histone reader involved in the response to DNA damage

Author

Kitevski-LeBlanc, Julianne, Fradet-Turcotte, Amélie, Kukic, Predrag, Wilson, Marcus D, Portella, Guillem, Yuwen, Tairan, Panier, Stephanie, Duan, Shili, Canny, Marella D, Van Ingen, Hugo, Arrowsmith, Cheryl H, Rubinstein, John L, Vendruscolo, Michele, Durocher, Daniel, and Kay, Lewis E

Subjects
Magnetic Resonance Spectroscopy, D. melanogaster, Ubiquitin-Protein Ligases, Cryoelectron Microscopy, Molecular Dynamics Simulation, 3. Good health, Histones, ubiquitin-based signalling, ubiquitylated-histone reader, biophysics, DNA damage, structural biology, Humans, DNA Breaks, Double-Stranded, human, Protein Binding
Abstract

Site-specific histone ubiquitylation plays a central role in orchestrating the response to DNA double-strand breaks (DSBs). DSBs elicit a cascade of events controlled by the ubiquitin ligase RNF168, which promotes the accumulation of repair factors such as 53BP1 and BRCA1 on the chromatin flanking the break site. RNF168 also promotes its own accumulation, and that of its paralog RNF169, but how they recognize ubiquitylated chromatin is unknown. Using methyl-TROSY solution NMR spectroscopy and molecular dynamics simulations, we present an atomic resolution model of human RNF169 binding to a ubiquitylated nucleosome, and validate it by electron cryomicroscopy. We establish that RNF169 binds to ubiquitylated H2A-Lys13/Lys15 in a manner that involves its canonical ubiquitin-binding helix and a pair of arginine-rich motifs that interact with the nucleosome acidic patch. This three-pronged interaction mechanism is distinct from that by which 53BP1 binds to ubiquitylated H2A-Lys15 highlighting the diversity in site-specific recognition of ubiquitylated nucleosomes.

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