Nature Structural & Molecular Biology Contents: 2014 Volume #21 pp 739-839

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TABLE OF CONTENTS September 2014 Volume 21, Issue 9 News and Views Review Articles Analysis Subscribe   Facebook   RSS   Recommend to library   Twitter   Advertisement nature.com webcasts Macmillan Science Communication presents a custom webcast on: Targeting the untargeted in translational research Thursday September 11, 2014 Session 1: Europe and the Middle East 2PM BST, 3pm CEST, 5PM GST Session 2: USA 9AM PDT, 11AM CDT, 12PM EDT  Register for the webcast and live Q and A session Sponsored by: Agilent   News and Views Top A peek into the atomic details of thalidomide's clinical effects   pp739 - 740 Sagar Bhogaraju and Ivan Dikic doi:10.1038/nsmb.2882 After being used in the 1950s to treat morning sickness in pregnant women, with devastating effects, thalidomide and its derivatives (lenalidomide and pomalidomide) are now widely used in cancer therapy. New structural work from two groups gives insights into the basis for the teratogenicity and other clinical effects of these drugs. See also: Article by Chamberlain et al. Closed for business: exit-channel coupling to active site conformation in bacterial RNA polymerase   pp741 - 742 Craig T Martin and Karsten Theis doi:10.1038/nsmb.2883 Fluorescent probes at the exit channel and near the active site of RNA polymerase shed light on how transcriptional pausing is regulated. See also: Article by Hein et al. Review The evolutionary journey of Argonaute proteins   pp743 - 753 Daan C Swarts, Kira Makarova, Yanli Wang, Kotaro Nakanishi, René F Ketting et al. doi:10.1038/nsmb.2879 Recent structural progress on prokaryotic and eukaryotic Argonaute proteins is reviewed here, along with the insights obtained into guide and target binding and target cleavage. Comprehensive phylogenetic analyses lead to a map of Argonaute's evolutionary paths, relating structural features and physiological roles. Structural & Molecular Biology JOBS of the week Research Technician in Molecular and Cell Biology (100%) ETH Zurich Postdoctoral Research Fellow in Immunology, Molecular Biology & Hemostaseology (m / f) University Medical Center - Mainz Postdoc in plant molecular / membrane protein biology University of Copenhagen Research Assistant The Ohio Stat University Medical Center Assistant Professor in Biology University of Delaware More Science jobs from Structural & Molecular Biology EVENT In Silico Drug Discovery Conference 03.12.14 Research Triangle Park, USA More science events from Articles Top Structure of Nipah virus unassembled nucleoprotein in complex with its viral chaperone   pp754 - 759 Filip Yabukarski, Philip Lawrence, Nicolas Tarbouriech, Jean-Marie Bourhis, Elise Delaforge et al. doi:10.1038/nsmb.2868 Replication of Nipah virus, which causes human encephalitis, requires delivery of viral nucleoprotein N to the viral genome by phosphoprotein chaperone, P. The crystal structure of the N0–P core complex now reveals how the chaperone prevents premature N assembly on RNA and identifies a potential target for antiviral drugs. NuRD–ZNF827 recruitment to telomeres creates a molecular scaffold for homologous recombination   pp760 - 770 Dimitri Conomos, Roger R Reddel and Hilda A Pickett doi:10.1038/nsmb.2877 Cancer cells lacking telomerase maintain telomere lengths required for cell growth through a recombination mechanism called ALT. Now, ALT-specific nuclear receptors are shown to recruit a zinc-finger protein that directs the nucleosome remodeler and histone deacetylase NuRD to telomeres to enhance homologous recombination. Structures of CRISPR Cas3 offer mechanistic insights into Cascade-activated DNA unwinding and degradation   pp771 - 777 Yanwu Huo, Ki Hyun Nam, Fang Ding, Heejin Lee, Lijie Wu et al. doi:10.1038/nsmb.2875 Type I CRISPR-Cas systems require a target-searching Cascade complex and the Cas3 degradation machine to drive prokaryotic adaptation to alien nucleic acids. Cas3 crystal structures now reveal the mechanism of concerted DNA unwinding and degradation. RBFOX and SUP-12 sandwich a G base to cooperatively regulate tissue-specific splicing   pp778 - 786 Kanako Kuwasako, Mari Takahashi, Satoru Unzai, Kengo Tsuda, Seiko Yoshikawa et al. doi:10.1038/nsmb.2870 Alternative pre-mRNA splicing is often jointly controlled by multiple splicing factors. Here Muto and colleagues elucidate the structural basis for cooperative RNA recognition by two splicing regulators required for tissue-specific expression of C. elegans FGFR. A proton wire to couple aminoacyl-tRNA accommodation and peptide-bond formation on the ribosome   pp787 - 793 Yury S Polikanov, Thomas A Steitz and C Axel Innis doi:10.1038/nsmb.2871 High-resolution structures of the 70S ribosome from Thermus thermophilus reveal a network of ordered waters in the peptidyl transferase center that suggests a mechanism for proton movement and formation and breakdown of the tetrahedral intermediate. RNA polymerase pausing and nascent-RNA structure formation are linked through clamp-domain movement   pp794 - 802 Pyae P Hein, Kellie E Kolb, Tricia Windgassen, Michael J Bellecourt, Seth A Darst et al. doi:10.1038/nsmb.2867 A combination of fluorescence and cross-linking assays are used to elucidate the reciprocal effects of RNA polymerase pausing and the secondary structure of the nascent transcript as it emerges from the translocating enzyme's RNA-exit channel. See also: News and Views by Martin & Theis Structure of the human Cereblon–DDB1–lenalidomide complex reveals basis for responsiveness to thalidomide analogs   pp803 - 809 Philip P Chamberlain, Antonia Lopez-Girona, Karen Miller, Gilles Carmel, Barbra Pagarigan et al. doi:10.1038/nsmb.2874 The protein Cereblon, part of an ubiquitin E3 ligase complex, is the target for anticancer thalidomide analogs. The crystal structure of human Cereblon-DDB1 with bound lenalidomide reveals how the drug affects E3 substrate recruitment. See also: News and Views by Bhogaraju & Dikic Architecture of the Saccharomyces cerevisiae RNA polymerase I Core Factor complex   pp810 - 816 Bruce A Knutson, Jie Luo, Jeffrey Ranish and Steven Hahn doi:10.1038/nsmb.2873 Chemical cross-linking MS and supporting biochemical and genetic analyses reveal the architecture of the yeast Core Factor complex and suggest how it directs transcription of RNA Pol I at rDNA promoters. EF-G catalyzes tRNA translocation by disrupting interactions between decoding center and codon–anticodon duplex   pp817 - 824 Guangqiao Liu, Guangtao Song, Danyang Zhang, Dejiu Zhang, Zhikai Li et al. doi:10.1038/nsmb.2869 EF-G catalyzes translocation of tRNA–mRNA in the ribosome. Biochemical and structural analyses of EF-G indicate that EF-G disrupts interactions between the decoding center and the codon–anticodon duplex that constitute the barrier for translocation. Regulation of microRNA-mediated gene silencing by microRNA precursors   pp825 - 832 Biswajoy Roy-Chaudhuri, Paul N Valdmanis, Yue Zhang, Qing Wang, Qing-Jun Luo et al. doi:10.1038/nsmb.2862 The precursor for miRNA-151 is found to compete with mature forms for target sites on E2f6 mRNA but not on a different mRNA. These findings indicate that miRNA processing can affect individual mRNA targets differently. Analysis Top Asymmetric mRNA localization contributes to fidelity and sensitivity of spatially localized systems   pp833 - 839 Robert J Weatheritt, Toby J Gibson and M Madan Babu doi:10.1038/nsmb.2876 A systematic analysis reveals features of proteins synthesized at distal locations owing to mRNA localization, including the presence of intrinsically disordered segments and assembly-promoting modules. These findings suggest that asymmetric protein distribution enhances interaction fidelity. Top Advertisement Nature at War: A special collection of articles originally published between 1914 and 1918.  Science and technology played a key role in World War One. A century later, a selection of articles from our archive reveals how Nature reported and analyzed these developments at the time.  Purchase and download this exclusive PDF for only $1.99.   Natureevents is a fully searchable, multi-disciplinary database designed to maximise exposure for events organisers. 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