Nature Structural & Molecular Biology Contents: 2015 Volume #22 pp 751-831

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TABLE OF CONTENTS October 2015 Volume 22, Issue 10 Editorial News and Views Articles Subscribe   Facebook   RSS   Recommend to library   Twitter   Advertisement Nature Microbiology: Call for Papers Launching in January 2016, Nature Microbiology is now open for submissions and inviting high-quality submissions. The journal will cover all aspects of microorganisms be it their evolution, physiology and cell biology, their interactions with each other, with a host, with an environment, or their societal significance.  Submit your next research paper to the journal.     Editorial Top Source-ful science   p751 doi:10.1038/nsmb.3110 Sharing source data—the actual measurements and unprocessed images behind the graphical representations used in figures—helps to ensure transparency and reproducibility of research results. We urge our authors to submit and share the source data with their published papers. News and Views Top Solute carriers keep on rockin'   pp752 - 754 Reinhart A F Reithmeier and Trevor F Moraes doi:10.1038/nsmb.3104 The crystal structure of a prokaryotic proton-driven fumarate transporter, the first for the diverse SLC26 transporter family, reveals a rare transmembrane-segment topology. The opposite orientation of two short central helices leads to the formation of a dipole-mediated anion-binding site, which is made alternately accessible to either side of the membrane through the rocking movement of the core and gate domains of the transporter. See also: Article by Geertsma et al. Molecular prejudice: RNA discrimination against purines allows response to a cellular alarm   pp754 - 756 Marisa D Ruehle and Jeffrey S Kieft doi:10.1038/nsmb.3095 The cellular 'alarmone' molecule ZTP accumulates when a critical cellular metabolic pathway is starved for substrate. The high-resolution structure of ZTP bound to its RNA-based sensor reveals unexpected strategies used by RNA to specifically recognize small-molecule ligands within the complex cellular mixture. SEC-uring membrane fusion: a sneak peek at SNARE-complex assembly driven by Sec1-Munc18 proteins   pp756 - 758 Brett M Collins and Jennifer L Martin doi:10.1038/nsmb.3094 How is cellular cargo delivered at the right time and the right place, in response to the right signal? A key new piece in this fascinating biological puzzle has just been revealed. Reversible aggregation after heat shock   p758 Katrina Woolcock doi:10.1038/nsmb.3109 Structural & Molecular Biology JOBS of the week NIDDK / NIH Post-Doctoral Fellowship position National Institutes of Health Diabetes, Endocrinology, and Obesity Branch (DEOB) Assistant Professor of Molecular Biophysics University of California San Diego Postdoctoral Fellow - Inflammation Amgen Assistant Professor, Stem Cell Genomics University of California, Santa Cruz Postdoctoral Fellow The University of Tennessee Health Science Center More Science jobs from Structural & Molecular Biology EVENT More science events from Articles Top Histone monoubiquitination by Clock-Bmal1 complex marks Per1 and Per2 genes for circadian feedback   pp759 - 766 Alfred G Tamayo, Hao A Duong, Maria S Robles, Matthias Mann and Charles J Weitz doi:10.1038/nsmb.3076 New data show that Clock-Bmal1, the central transcriptional activator that drives expression of circadian target genes, also recruits the Ddb1-Cullin-4 ubiquitin ligase to clock promoters to enhance the subsequent binding of the feedback repressors that generate the circadian periodicity of gene expression. Translational arrest by a prokaryotic signal recognition particle is mediated by RNA interactions   pp767 - 773 Bertrand Beckert, Alexej Kedrov, Daniel Sohmen, Georg Kempf, Klemens Wild et al. doi:10.1038/nsmb.3086 Cryo-EM analysis of a bacterial SRP reveals that, differently from eukaryotic SRP, it interacts with the ribosome via contacts between the 6S RNA and the 23S rRNA to mediate translational slowdown. Linker Nups connect the nuclear pore complex inner ring with the outer ring and transport channel   pp774 - 781 Jessica Fischer, Roman Teimer, Stefan Amlacher, Ruth Kunze and Ed Hurt doi:10.1038/nsmb.3084 An in vitro-reconstitution approach reveals the interactions between nuclear pore complex modules. Short motifs within linker nucleoporins connect the inner-pore-ring complex with subcomplexes of the outer ring and the transport channel. Structural basis for specific recognition of single-stranded RNA by Toll-like receptor 13   pp782 - 787 Wen Song, Jia Wang, Zhifu Han, Yifan Zhang, Heqiao Zhang, Jiawei Wang, Hong-Wei Wang & Jijie Chai doi:10.1038/nsmb.3080 Crystallographic and cryo-EM analyses using short synthetic single-stranded RNAs unveil the structural basis for recognition of bacterial 23S rRNA and vesicular stomatitis virus by Toll-like receptor 13, which triggers an immune response. Structure-based energetics of protein interfaces guides foot-and-mouth disease virus vaccine design   pp788 - 794 Abhay Kotecha, Julian Seago, Katherine Scott, Alison Burman, Silvia Loureiro, Jingshan Ren, Claudine Porta, Helen M Ginn, Terry Jackson, Eva Perez-Martin, C Alistair Siebert, Guntram Paul, Juha T Huiskonen, Ian M Jones, Robert M Esnouf, Elizabeth E Fry, Francois F Maree, Bryan Charleston & David I Stuart doi:10.1038/nsmb.3096 Foot-and-mouth disease virus (FMDV) capsids are often unstable, thus limiting their use as vaccines. A computational method was used to strengthen protein-protein interfaces and engineer stabilized FMDV capsids, which generated improved antibody responses in vaccinated calves and guinea pigs. Impact of holdase chaperones Skp and SurA on the folding of β-barrel outer-membrane proteins   pp795 - 802 Johannes Thöma, Bjorn M Burmann, Sebastian Hiller and Daniel J Müller doi:10.1038/nsmb.3087 AFM and NMR are used to observe how the chaperones Skp and SurA work to fold a β-barrel outer-membrane protein, FhuA. Skp maintains FhuA in an unfolded state, and Sur A facilitates its folding. Structure of a prokaryotic fumarate transporter reveals the architecture of the SLC26 family   pp803 - 808 Eric R Geertsma, Yung-Ning Chang, Farooque R Shaik, Yvonne Neldner, Els Pardon,Jan Steyaert & Raimund Dutzler doi:10.1038/nsmb.3091 SLC26 membrane proteins constitute a large family of anion transporters with diverse functions. The first structure of a full-length SLC26 transporter now provides a common framework for the architecture of this protein family. See also: News and Views by Reithmeier & Moraes Structure and multistate function of the transmembrane electron transporter CcdA   pp809 - 814 Jessica A Williamson, Seung-Hyun Cho, Jiqing Ye, Jean-Francois Collet, Jonathan R Beckwith & James J Chou doi:10.1038/nsmb.3099 Solution NMR and functional analyses reveal the 3D structure of a transmembrane reductase, the archeal CcdA, and suggest a mechanism for how these enzymes relay electrons across cell membranes. Synaptotagmin-1 binds to PIP2-containing membrane but not to SNAREs at physiological ionic strength   pp815 - 823 Yongsoo Park, Jong Bae Seo, Alicia Fraind, Angel Pérez-Lara, Halenur Yavuz,Kyungreem Han, Seung-Ryoung Jung, Iman Kattan, Peter Jomo Walla, MooYoung Choi, David S Cafiso, Duk-Su Koh & Reinhard Jahn doi:10.1038/nsmb.3097 Concentrations of cations and ATP affect the binding activities of synaptotagmin-1, to trigger synaptic vesicle exocytosis. In physiological ionic conditions, synaptotagmin-1's interaction with SNARE proteins is prevented, and its binding is confined to PIP2-containing membrane. miR-128 represses L1 retrotransposition by binding directly to L1 RNA   pp824 - 831 Matthias Hamdorf, Adam Idica, Dimitrios G Zisoulis, Lindsay Gamelin, Charles Martin,Katie J Sanders & Irene M Pedersen doi:10.1038/nsmb.3090 In somatic cells, L1 retrotransposition is kept in check by DNA methylation. However, in hypomethylated cells, such as cancer cells or iPSCs, miR-128 represses new retrotransposition events and thus might aid in maintaining genome stability. Top Advertisement Nature Plants: Call for Papers Nature Plants launched in January and covers all aspects of plants be it their evolution, genetics, development or metabolism, their interactions with the environment, or their societal significance. 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