Nature Structural & Molecular Biology Contents: 2015 Volume #22 pp 833-939

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TABLE OF CONTENTS November 2015 Volume 22, Issue 11 Focus Correspondence News and Views Editorial Commentary Perspectives Reviews Articles Erratum Corrigendum 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.     Focus Top Focus on Telomeres Focus issue: November 2015 Volume 22 No 11 Contents Editorial Commentary Perspectives Reviews Related content Sponsor Correspondence Top Privateer: software for the conformational validation of carbohydrate structures   pp833 - 834 Jon Agirre, Javier Iglesias-Fernández, Carme Rovira, Gideon J Davies, Keith S Wilson et al. doi:10.1038/nsmb.3115 News and Views Top Protein-RNA interaction restricts telomerase from running through the stop sign   pp835 - 836 Linghe Xi and Thomas R Cech doi:10.1038/nsmb.3118 Telomerase is a unique reverse transcriptase in that it repetitively uses a short piece of its RNA component as template to synthesize DNA. A new crystal structure of a part of the Tetrahymena telomerase ribonucleoprotein reveals how reverse transcription is limited to this specific template region. See also: Article by Jansson et al. Ribosomal 60S-subunit production: the final scene   pp837 - 838 Celia Plisson-Chastang, Natacha Larburu and Pierre-Emmanuel Gleizes doi:10.1038/nsmb.3121 Newly synthesized 60S ribosomal subunits are licensed for translation through the release of the antiassociation factor eIF6. A new study shows by cryo-electron microscopy how eIF6 eviction results from a long-range allosteric cascade that involves SBDS, the protein mutated in Shwachman-Diamond syndrome. See also: Article by Weis et al. | Article by Chaker-Margot et al. Structural & Molecular Biology JOBS of the week Faculty Position at Yale University, Department of Molecular, Cellular and Developmental Biology Yale University Assistant Professor - Biochemistry, Biophysics, Molecular Biology, Genetics University of Toronto Assistant Professors in Molecular Animal Physiology and Plant Biology / Evolution National Institute of Education More Science jobs from Editorial Top Focus on Telomeres Unraveling the ends   p843 doi:10.1038/nsmb.3123 Deciphering the complexity of events at telomeres has enhanced understanding of how telomeres function to maintain genome integrity and how their dysfunction gives rise to human disease. Commentary Top Focus on Telomeres A DNA-hairpin model for repeat-addition processivity in telomere synthesis   pp844 - 847 Wei Yang and Young-Sam Lee doi:10.1038/nsmb.3098 Telomerase is a nucleoprotein complex of a reverse transcriptase and an RNA that binds complementary telomeric-repeat DNA sequences and directs their extension. In this Commentary, the authors propose how hairpin structures formed by telomeric DNA repeats promote addition of telomerase repeats and why telomere sequences are evolutionarily conserved despite the problems that they pose to DNA replication. Perspectives Top Focus on Telomeres Control of telomerase action at human telomeres   pp848 - 852 Dirk Hockemeyer and Kathleen Collins doi:10.1038/nsmb.3083 Telomerase recruitment and activity are regulated by telomere-bound proteins that protect the chromosome ends. In this Perspective, the authors discuss recent advances in understanding how the interactions of shelterin and telomerase components contribute to telomere-length homeostasis. Focus on Telomeres TERRA and the state of the telomere   pp853 - 858 Karsten Rippe and Brian Luke doi:10.1038/nsmb.3078 Transcription of telomeres generates long noncoding RNAs (lncRNAs) composed of telomeric repeat sequences (TERRA) that hybridize with telomeric DNA and are components of telomeric heterochromatin. This Perspective considers the physiological roles of TERRA in telomere homeostasis and proposes that TERRA's functions are determined by the state of its telomere targets. Reviews Top Focus on Telomeres Complex interactions between the DNA-damage response and mammalian telomeres   pp859 - 866 Nausica Arnoult and Jan Karlseder doi:10.1038/nsmb.3092 The shelterin complex sequesters the linear ends of chromosomes and prevents telomeres from being recognized as DNA double-strand breaks. In this Review, the authors discuss the complex interactions between shelterin components and DNA damage-response factors and consider shelterin's emerging roles as regulators of genome integrity and cell fate. Focus on Telomeres Molecular basis of telomere dysfunction in human genetic diseases   pp867 - 874 Grzegorz Sarek, Paulina Marzec, Pol Margalef and Simon J Boulton doi:10.1038/nsmb.3093 Genetic mutations that compromise telomere-length maintenance give rise to a group of related human diseases called telomere biology disorders. This Review discusses the molecular functions impaired by disease-associated mutations as well as modes of inheritance and clinical manifestations. Focus on Telomeres Molecular mechanisms of activity and derepression of alternative lengthening of telomeres   pp875 - 880 Hilda A Pickett and Roger R Reddel doi:10.1038/nsmb.3106 Cancer cells that lack telomerase activity can maintain telomere lengths that permit continued proliferation via a recombination-based pathway called alternative lengthening of telomeres (ALT). This Review summarizes recent insights into the mechanism of ALT function and how it is repressed in normal cells to permit telomere attrition that limits replication. Articles Top Structural basis of template-boundary definition in Tetrahymena telomerase   pp883 - 888 Linnea I Jansson, Ben M Akiyama, Alexandra Ooms, Cheng Lu, Seth M Rubin et al. doi:10.1038/nsmb.3101 A crystal structure of the RNA-binding domain of Tetrahymena telomerase reverse transcriptase (TERT) with its template RNA (TER) reveals interactions that establish the template boundary element and direct the addition of telomeric DNA repeats. See also: News and Views by Xi & Cech Rif1 binds to G quadruplexes and suppresses replication over long distances   pp889 - 897 Yutaka Kanoh, Seiji Matsumoto, Rino Fukatsu, Naoko Kakusho, Nobuaki Kono et al. doi:10.1038/nsmb.3102 ChIP-seq, biochemical and in vivo assays show that Rif1 binds G-rich motifs that can form G-quadruplex structures, thus regulating firing of proximal and distal DNA replication origins in fission yeast. The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client   pp898 - 905 Andi Mainz, Jirka Peschek, Maria Stavropoulou, Katrin C Back, Benjamin Bardiaux et al. doi:10.1038/nsmb.3108 Solid-state and solution NMR spectroscopy provide insights into the chaperone αB-crystallin's highly dynamic assembly, which is instrumental in its distinct interactions with a wide range of structurally variable clients. HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions   pp906 - 913 Yanqing Zhang, Chandra Sekhar Mandava, Wei Cao, Xiaojing Li, Dejiu Zhang et al. doi:10.1038/nsmb.3103 The E. coli GTPase HflX promotes ribosomal-subunit dissociation by inducing conformational changes in central intersubunit bridges and thereby rescues stalled ribosomes under heat-shock conditions. Mechanism of eIF6 release from the nascent 60S ribosomal subunit   pp914 - 919 Felix Weis, Emmanuel Giudice, Mark Churcher, Li Jin, Christine Hilcenko et al. doi:10.1038/nsmb.3112 During eukaryotic ribosome biogenesis, the nascent 60S subunit is activated by SBDS and GTPase EFL1. Cryo-EM and mutational analyses reveal how SBDS-EFL1 evicts antiassociation factor eIF6 from 60S and explain the effects of disease-related SBDS mutations. See also: News and Views by Plisson-Chastang et al. Stage-specific assembly events of the 6-MDa small-subunit processome initiate eukaryotic ribosome biogenesis   pp920 - 923 Malik Chaker-Margot, Mirjam Hunziker, Jonas Barandun, Brian D Dill and Sebastian Klinge doi:10.1038/nsmb.3111 Proteomics approach using MS2 as an RNA tag is used to provide snapshots of nascent preribosomal particles from budding yeast, thus allowing the determination of the stage-specific order in which 70 ribosome-assembly factors associate with pre-rRNA domains. See also: News and Views by Plisson-Chastang et al. Capturing snapshots of APE1 processing DNA damage   pp924 - 931 Bret D Freudenthal, William A Beard, Matthew J Cuneo, Nadezhda S Dyrkheeva and Samuel H Wilson doi:10.1038/nsmb.3105 New crystal structures of the human endonuclease APE1 bound to substrate and product DNAs reveal the mechanism of recognition and processing of apurinic-apyrimidinic (AP) sites during base excision repair. Polymerase δ replicates both strands after homologous recombination-dependent fork restart   pp932 - 938 Izumi Miyabe, Ken'Ichi Mizuno, Andrea Keszthelyi, Yasukazu Daigaku, Meliti Skouteri et al. doi:10.1038/nsmb.3100 New analyses in S. pombe show that both the leading and lagging strands are replicated by DNA polymerase δ when stalled replication forks use homologous recombination to restart semiconservative DNA synthesis. Erratum Top Erratum: Plasmepsin V shows its carnivorous side   p939 Daniel E Goldberg doi:10.1038/nsmb1115-939a Corrigendum Top Corrigendum: Structure and multistate function of the transmembrane electron transporter CcdA   p939 Jessica A Williamson, Seung-Hyun Cho, Jiqing Ye, Jean-Francois Collet, Jonathan R Beckwith et al. doi:10.1038/nsmb1115-939b 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. The journal welcomes high quality submissions and encourages you and your colleagues to consider submitting your next research paper to the journal.  Submit your next research paper to the journal.     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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