Nature Structural & Molecular Biology Contents: 2015 Volume #22 pp 99-174

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TABLE OF CONTENTS February 2015 Volume 22, Issue 2 News and Views Research Highlights Articles Subscribe   Facebook   RSS   Recommend to library   Twitter   Advertisement Don't let your data go to waste... Scientific Data helps researchers make the most of their data, offering publication in a peer reviewed open access journal. We welcome data of all sizes, from all areas of science. What's unique? A new type of article providing detailed descriptions of scientifically valuable datasets, maximising data discoverability and reuse. Discover what we can do for your data     News and Views Top Synergistic activation of Toll-like receptor 8 by two RNA degradation products   pp99 - 101 Matthias Geyer, Karin Pelka and Eicke Latz doi:10.1038/nsmb.2967 Recognition of nucleic acids is a key strategy of the innate immune system to detect infectious organisms and tissue damage. Toll-like receptor (TLR) 8 was long assumed to be a receptor for single-stranded (ss) RNA. Unexpected findings now suggest that TLR8 recognizes RNA degradation products rather than ssRNA and that synergistic binding of two uridine-containing agonists at distinct sites of the receptor leads to activation of the innate immune response. See also: Article by Tanji et al. An enzyme cofactor with a split personality   pp101 - 103 Anthony Mittermaier doi:10.1038/nsmb.2968 Little is currently known about the molecular determinants of energy barriers along enzyme catalytic pathways. Kern and co-workers have studied this question in adenylate kinase (Adk) and now reveal that a single Mg2+ ion can accelerate two distinct steps, thus uncovering an unexpected dual role for this ubiquitous cofactor. See also: Article by Kerns et al. Designs on a curve   pp103 - 105 J Fernando Bazan and Andrey V Kajava doi:10.1038/nsmb.2966 The structural rules governing the curving folds of solenoid proteins, as distilled down to the level of the underlying sequence repeats, provide designers with the tools to reliably fashion new variants with tunable geometries. Bespoke leucine-rich repeat (LRR) scaffolds, as recognition proteins, can now be tailored to better fit their targets. See also: Article by Park et al. Muscling in on the ryanodine receptor   pp106 - 107 Ivana Y Kuo and Barbara E Ehrlich doi:10.1038/nsmb.2960 The ryanodine receptor (RyR), an ion channel regulating intracellular calcium release in excitable cells, has been challenging for structural analysis because of its colossal proportions compared to most other ion channels. Three independent groups have now used recent technological advancements in single-particle cryo-EM to make giant strides in solving the structure of this elusive protein complex. Structural & Molecular Biology JOBS of the week Biochemistry and Molecular Biology UT Southwestern Medical Center Postdoctoral Fellows University of Texas Health Science Center, San Antonio (UTHSCSA) More Science jobs from Structural & Molecular Biology EVENT Thiol-based redox switches in life sciences 18.09.15 Sant Feliu de Guixols, Spain More science events from Research Highlights Top Bringing phosphorylation into the fold | Histone acetylome mapped | Resolving stalled ribosomes Articles Top Toll-like receptor 8 senses degradation products of single-stranded RNA   pp109 - 115 Hiromi Tanji, Umeharu Ohto, Takuma Shibata, Masato Taoka, Yoshio Yamauchi et al. doi:10.1038/nsmb.2943 Toll-like receptors (TLRs) have key roles in innate immunity. Here, Shimizu and colleagues report crystal structures of TLR8 in complex with single-stranded RNA that reveal the molecular basis for recognition of a natural ligand. See also: News and Views by Geyer et al. K63 polyubiquitination is a new modulator of the oxidative stress response   pp116 - 123 Gustavo M Silva, Daniel Finley and Christine Vogel doi:10.1038/nsmb.2955 Oxidative stress induces a number of cellular responses. Silva et al. uncover a peroxide-mediated K63-linked polyubiquitination pathway, and identify its targets and regulators. The energy landscape of adenylate kinase during catalysis   pp124 - 131 S Jordan Kerns, Roman V Agafonov, Young-Jin Cho, Francesco Pontiggia, Renee Otten et al. doi:10.1038/nsmb.2941 Structural, computation and kinetics approaches reveal the energy landscape of catalysis by adenylate kinase and show that the cofactor Mg2+ activates two distinct molecular events in the reaction cycle: phosphoryl transfer and lid opening. See also: News and Views by Mittermaier Ring closure activates yeast γTuRC for species-specific microtubule nucleation   pp132 - 137 Justin M Kollman, Charles H Greenberg, Sam Li, Michelle Moritz, Alex Zelter et al. doi:10.1038/nsmb.2953 The γ-tubulin ring complex (γTuRC) nucleates microtubules in the cell. The functional, closed state of yeast γTuRC is now visualized, and its microtubule-nucleating activity is found to be species specific. The RNA helicase Aquarius exhibits structural adaptations mediating its recruitment to spliceosomes   pp138 - 144 Inessa De, Sergey Bessonov, Romina Hofele, Karine dos Santos, Cindy L Will et al. doi:10.1038/nsmb.2951 Aquarius is an RNA helicase associated with spliceosomes. Lührmann, Pena and colleagues now provide structural insights into how Aquarius is recruited to the spliceosome, revealing a new spliceosomal building block that aids in Aquarius positioning. Charge-driven dynamics of nascent-chain movement through the SecYEG translocon   pp145 - 149 Nurzian Ismail, Rickard Hedman, Martin Lindén and Gunnar von Heijne doi:10.1038/nsmb.2940 Proteins with charged amino acid residues encounter an electric force as they transit through membranes holding membrane potential. Von Heijne and colleagues measure this force to assess how membrane electrostatics contributes to translocation dynamics. CtIP tetramer assembly is required for DNA-end resection and repair   pp150 - 157 Owen R Davies, Josep V Forment, Meidai Sun, Rimma Belotserkovskaya, Julia Coates et al. doi:10.1038/nsmb.2937 CtIP helps maintain genomic stability by promoting DNA double-strand-break repair. Structural and biophysical analyses now show that the N terminus of human CtIP forms a tetrameric structure that is required for resection of broken DNA ends to permit their repair by homologous recombination. Tetrameric Ctp1 coordinates DNA binding and DNA bridging in DNA double-strand-break repair   pp158 - 166 Sara N Andres, C Denise Appel, James W Westmoreland, Jessica S Williams, Yvonne Nguyen et al. doi:10.1038/nsmb.2945 Structural, biophysical and genetic analyses reveal that Schizosaccharomyces pombe Ctp1 forms a flexible tetramer with multivalent DNA-binding and bridging activities that contribute to Ctp1's role in repair of DNA double-strand breaks. Control of repeat-protein curvature by computational protein design   pp167 - 174 Keunwan Park, Betty W Shen, Fabio Parmeggiani, Po-Ssu Huang, Barry L Stoddard et al. doi:10.1038/nsmb.2938 Leucine-rich repeats (LRRs) can form horseshoe-like structures with different curvatures in nature. A computational approach now allows the design of 12 new LRR proteins with precise curvatures, using defined building blocks and junction modules. See also: News and Views by Bazan & Kajava Top Advertisement Nature Structural & Molecular Biology Focus on Noncoding RNAs In a special Focus issue, Nature Structural & Molecular Biology explores the functional diversity of noncoding RNAs in various cellular processes, the molecular mechanisms of different RNA-interference pathways and the latest breakthroughs in RNA technology.  Click here to access this special Focus issue!     Natureevents is a fully searchable, multi-disciplinary database designed to maximise exposure for events organisers. The contents of the Natureevents Directory are now live. The digital version is available here. Find the latest scientific conferences, courses, meetings and symposia on natureevents.com. For event advertising opportunities across the Nature Publishing Group portfolio please contact natureevents@nature.com More Nature Events

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