Focus
Focus on Chaperones and Chaperonins
The 2011 Albert Lasker Basic Medical Research Award honors F. Ulrich Hartl and Arthur L. Horwich, for their "discoveries concerning the cell's protein-folding machinery, exemplified by cage-like structures that convert newly made proteins into their biologically active forms." We celebrate the award by presenting a collection of recent papers on chaperones and chaperonins published in NSMB. We also call your attention to our 2009 Focus on Protein Folding.
Current Research
Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco-
Andreas Bracher, Amanda Starling-Windhof, F Ulrich Hartl & Manajit Hayer-Hartl
Nature Structural & Molecular Biology 18, 875-880 (2011)
doi:10.1038/nsmb.2090
Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53-
Franz Hagn, Stephan Lagleder, Marco Retzlaff, Julia Rohrberg, Oliver Demmer, Klaus Richter, Johannes Buchner & Horst Kessler
Nature Structural & Molecular Biology, advance online publication: 04 September 2011
doi:10.1038/nsmb.2114
The client protein p53 adopts a molten globule-like state in the presence of Hsp90-
Sung Jean Park, Brendan N Borin, Maria A Martinez-Yamout & H Jane Dyson
Nature Structural & Molecular Biology 18, 537-541 (2011)
doi:10.1038/nsmb.2045
Genetic selection designed to stabilize proteins uncovers a chaperone called Spy-
Shu Quan, Philipp Koldewey, Tim Tapley, Nadine Kirsch, Karen M Ruane, Jennifer Pfizenmaier, Rong Shi, Stephan Hofmann, Linda Foit, Guoping Ren, Ursula Jakob, Zhaohui Xu, Miroslaw Cygler & James C A Bardwell
Nature Structural & Molecular Biology 18, 262-269 (2011)
doi:10.1038/nsmb.2016
Mechanics of Hsp70 chaperones enables differential interaction with client proteins-
Rainer Schlecht, Annette H Erbse, Bernd Bukau & Matthias P Mayer
Nature Structural & Molecular Biology 18, 345-351 (2011)
doi:10.1038/nsmb.2006
Single-molecule analysis of a molecular disassemblase reveals the mechanism of Hsc70-driven clathrin uncoating-
Till Böcking, François Aguet, Stephen C Harrison & Tomas Kirchhausen
Nature Structural & Molecular Biology 18, 295-301 (2011)
doi:10.1038/nsmb.1985
Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions-
Moritz Marcinowski, Matthias Höller, Matthias J Feige, Danae Baerend, Don C Lamb & Johannes Buchner
Nature Structural & Molecular Biology 18, 150-158 (2011)
doi:10.1038/nsmb.1970
Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle-
Jing Li, Klaus Richter & Johannes Buchner
Nature Structural & Molecular Biology 18, 61-66 (2011)
doi:10.1038/nsmb.1965
Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin-
Inés G Muñoz, Hugo Yébenes, Min Zhou, Pablo Mesa, Marina Serna, Ah Young Park, Elisabeth Bragado-Nilsson, Ana Beloso, Guillermo de Cárcer, Marcos Malumbres, Carol V Robinson, José M Valpuesta & Guillermo Montoya
Nature Structural & Molecular Biology 18, 14-19 (2011)
doi:10.1038/nsmb.1971
Solid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomers-
Stefan Jehle, Ponni Rajagopal, Benjamin Bardiaux, Stefan Markovic, Ronald Kühne, Joseph R Stout, Victoria A Higman, Rachel E Klevit, Barth-Jan van Rossum & Hartmut Oschkinat
Nature Structural & Molecular Biology 17, 1037-1042 (2010)
doi:10.1038/nsmb.1891
Determinants of structural and functional plasticity of a widely conserved protease chaperone complex-
Melisa Merdanovic, Nicolette Mamant, Michael Meltzer, Simon Poepsel, Alexandra Auckenthaler, Rie Melgaard, Patrick Hauske, Luitgard Nagel-Steger, Anthony R Clarke, Markus Kaiser, Robert Huber & Michael Ehrmann
Nature Structural & Molecular Biology 17, 837-843 (2010)
doi:10.1038/nsmb.1839
The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation-
Stephen Tam, Christoph Spiess, William Auyeung, Lukasz Joachimiak, Bryan Chen, Michelle A Poirier & Judith Frydman
Nature Structural & Molecular Biology 16, 1279-1285 (2009)
doi:10.1038/nsmb.1700
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