Nature Structural & Molecular Biology Contents: 2015 Volume #22 pp 433-508

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TABLE OF CONTENTS June 2015 Volume 22, Issue 6 Correspondence News and Views Research Highlights Articles Brief Communication Subscribe   Facebook   RSS   Recommend to library   Twitter   Advertisement New to NPG from Apr 2015 Co-published by Shanghai Institutes for Biological Sciences (SIBS), Chinese Academy of Sciences (CAS) and Nature Publishing Group, Sister Journal to Cell Research. Cell Discovery is a new online open access, fully peer-reviewed journal publishes results of significance and originality in all areas of molecular & cell biology.  Discover more about Cell Discovery   Correspondence Top NMR Exchange Format: a unified and open standard for representation of NMR restraint data OPEN   pp433 - 434 Aleksandras Gutmanas, Paul D Adams, Benjamin Bardiaux, Helen M Berman, David A Case, Rasmus H Fogh, Peter Güntert, Pieter M S Hendrickx, Torsten Herrmann, Gerard J Kleywegt, Naohiro Kobayashi, Oliver F Lange, John L Markley, Gaetano T Montelione, Michael Nilges, Timothy J Ragan, Charles D Schwieters, Roberto Tejero, Eldon L Ulrich, Sameer Velankar, Wim F Vranken, Jonathan R Wedell, John Westbrook, David S Wishart and Geerten W Vuister doi:10.1038/nsmb.3041 News and Views Top Grab the wiggly tail: new insights into the dynamics of circadian clocks   pp435 - 436 Ka Yi Hui and Jürgen A Ripperger doi:10.1038/nsmb.3039 How do molecular interactions determine the period length of a circadian oscillator? In mammals, a disordered region of the BMAL1 transcription factor that is able to interact with activators or repressors seems to perform this function. See also: Article by Xu et al. Exposing the secrets of sex determination   pp437 - 438 Remo Rohs, Ana Carolina Dantas Machado and Lin Yang doi:10.1038/nsmb.3042 Sex-determining transcription factors recognize their genomic target sites through mechanisms of DNA base-and-shape readout in combination with cooperative binding. Murphy et al. reveal that for one such transcription factor, DMRT1, the DNA sequence-and-shape features of its binding sites determine whether it binds DNA as a dimer, trimer or tetramer; they also characterize protein-DNA contacts that affect gender phenotypes in flies and humans. See also: Article by Murphy et al. RGM co-receptors add complexity to BMP signaling   pp439 - 440 Thomas D Mueller doi:10.1038/nsmb.3037 Ten years ago, the repulsive guidance molecules (RGMs), a family of three glycosylphosphatidylinositol-anchored glycoproteins, were identified as highly specific co-receptors of the bone morphogenetic proteins (BMPs). Newly reported crystal structures provide exciting insights into how RGM co-receptors may modulate BMP signaling. See also: Article by Healey et al. Research Highlights A-form DNA for survival | An unexpected role for mitochondrial ClpX | The ghost in the machine Structural & Molecular Biology JOBS of the week PhD position in Molecular Biology - Structural biology of proteins involved in circadian rhythms & DNA replication Institute of Molecular Biology (IMB) Mainz Post-Doctoral Positions – Structural Biology Memorial Sloan Kettering Cancer Center (MSKCC) Exciting PhD Positions in Modern Biology VBC PhD Programme Post-Doctoral Fellow, Screening The Centre for Drug Research and Development More Science jobs from Structural & Molecular Biology EVENT 40th FEBS Congress – The Biochemical Basis of Life 04.07.15 Berlin, Germany More science events from Articles Top An ancient protein-DNA interaction underlying metazoan sex determination   pp442 - 451 Mark W Murphy, John K Lee, Sandra Rojo, Micah D Gearhart, Kayo Kurahashi, Surajit Banerjee, Guy-André Loeuille, Anu Bashamboo, Kenneth McElreavey, David Zarkower, Hideki Aihara and Vivian J Bardwell doi:10.1038/nsmb.3032 DMRT transcription factors, key regulators of metazoan sexual development, use a unique DNA binding mode critical for male-to-female sex reversal in humans. See also: News and Views by Rohs et al. A dynamic DNA-repair complex observed by correlative single-molecule nanomanipulation and fluorescence   pp452 - 457 Evan T Graves, Camille Duboc, Jun Fan, François Stransky, Mathieu Leroux-Coyau and Terence R Strick doi:10.1038/nsmb.3019 Single-molecule imaging reveals how stalled Escherichia coli RNA polymerase is displaced by the superfamily 2 DNA translocase (SF2) repair factor Mfd to permit transcription-coupled DNA repair. Repulsive guidance molecule is a structural bridge between neogenin and bone morphogenetic protein   pp458 - 465 Eleanor G Healey, Benjamin Bishop, Jonathan Elegheert, Christian H Bell, Sergi Padilla-Parra and Christian Siebold doi:10.1038/nsmb.3016 Structural and functional analyses reveal how human repulsive-guidance-molecule glycoproteins activate bone morphogenic protein (BMP) signaling and physically link the latter to the neogenin pathway. See also: News and Views by Mueller The mechanism of inhibition of protein synthesis by the proline-rich peptide oncocin   pp466 - 469 Raktim N Roy, Ivan B Lomakin, Matthieu G Gagnon and Thomas A Steitz doi:10.1038/nsmb.3031 The crystal structure of the thermophilic 70S ribosome bound to the antimicrobial peptide Onc112 reveals that the peptide interacts with three adjacent functional sites in the ribosome. The proline-rich antimicrobial peptide Onc112 inhibits translation by blocking and destabilizing the initiation complex   pp470 - 475 A Carolin Seefeldt, Fabian Nguyen, Stéphanie Antunes, Natacha Pérébaskine, Michael Graf, Stefan Arenz, K Kishore Inampudi, Céline Douat, Gilles Guichard, Daniel N Wilson and C Axel Innis doi:10.1038/nsmb.3034 Structural and biochemical studies reveal how the antimicrobial peptide Onc112 binds to bacterial ribosomes and show that Onc112 blocks and destabilizes the translation-initiation complex. Cryptochrome 1 regulates the circadian clock through dynamic interactions with the BMAL1 C terminus   pp476 - 484 Haiyan Xu, Chelsea L Gustafson, Patrick J Sammons, Sanjoy K Khan, Nicole C Parsley, Chidambaram Ramanathan, Hsiau-Wei Lee, Andrew C Liu & Carrie L Partch doi:10.1038/nsmb.3018 The mammalian circadian cycle is determined by sequential activation of clock target-gene expression by CLOCK-BMAL and subsequent repression by CRY. Biochemical and NMR data now show that Cry1 competes with coactivators for binding to the BMAL1 transcriptional-activation domain to regulate circadian cycling. See also: News and Views by Hui & Ripperger Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G   pp485 - 491 Takahide Kouno, Elizabeth M Luengas, Megumi Shigematsu, Shivender M D Shandilya, JingYing Zhang, Luan Chen, Mayuko Hara, Celia A Schiffer, Reuben S Harris and Hiroshi Matsuo doi:10.1038/nsmb.3033 Evolution- and structure-guided mutagenesis allows elucidation of the solution NMR structure of the N-terminal domain of APOBEC3G. Mapping of HIV-1 Vif binding to the APOBEC3G NTD reveals an interaction interface distinct from those in other APOBEC3 proteins. Vps4 disassembles an ESCRT-III filament by global unfolding and processive translocation   pp492 - 498 Bei Yang, Goran Stjepanovic, Qingtao Shen, Andreas Martin and James H Hurley doi:10.1038/nsmb.3015 HDX-MS and cross-linking analyses by Hurley and colleagues reveal that the AAA+ ATPase Vps4 disassembles a substrate by global unfolding and translocation through its central pore, in a mechanism reminiscent of that of the unfoldase ClpX. Aβ(1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease   pp499 - 505 YYiling Xiao, Buyong Ma, Dan McElheny, Sudhakar Parthasarathy, Fei Long, Minako Hoshi, Ruth Nussinov and Yoshitaka Ishii doi:10.1038/nsmb.2991 Aβ(1-42) is the most pathogenic amyloid-β species in Alzheimer's disease (AD). The solid-state NMR-based atomic model of an Aβ(1-42) fibril elucidates the mechanism of fibril formation and propagation in AD and other amyloid diseases. Advertisement Nature Communications is now fully open access All new submissions if accepted, will be published open access and an article processing charge will apply. For more information visit the website. Visit our open access funding page or contact openaccess@nature.com to learn more on APC funding.   Brief Communication Top X-ray structures of Drosophila dopamine transporter in complex with nisoxetine and reboxetine   pp506 - 508 Aravind Penmatsa, Kevin H Wang and Eric Gouaux doi:10.1038/nsmb.3029 Crystal structures of the Drosophila melanogaster dopamine transporter dDAT in complex with inhibitors reboxetine and nisoxetine shed light on the molecular basis of antidepressant selectivity and specificity. Top 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. 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