Nature Structural & Molecular Biology Contents: 2015 Volume #22 pp 587-645

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TABLE OF CONTENTS August 2015 Volume 22, Issue 8 News and Views Articles Brief Communication 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.     News and Views Top MCM2 binding to histones H3-H4 and ASF1 supports a tetramer-to-dimer model for histone inheritance at the replication fork   pp587 - 589 Camille Clément and Geneviève Almouzni doi:10.1038/nsmb.3067 MCM2, a component of the replicative helicase, can bind histones H3-H4 in both tetrameric and dimeric form, depending on the presence of the histone chaperone ASF1. A structural analysis of the complexes now sheds light on key domains in the MCM2 protein that prove important for cell proliferation. See also: Article by Huang et al. Articles Structural basis for plasmepsin V inhibition that blocks export of malaria proteins to human erythrocytes   pp590 - 596 Anthony N Hodder, Brad E Sleebs, Peter E Czabotar, Michelle Gazdik, Yibin Xu ,Matthew T O'Neill, Sash Lopaticki, Thomas Nebl, Tony Triglia, Brian J Smith, Kym Lowes, Justin A Boddey & Alan F Cowman doi:10.1038/nsmb.3061 Plasmepsin V is an aspartyl protease essential for export of effector proteins to Plasmodium-infected erythrocytes. A new inhibitor blocks plasmepsin V and inhibits parasite growth; it has also allowed solving the structure of P. vivax plasmepsin V. Structural & Molecular Biology JOBS of the week Professor of Lipid and Membrane Biology (211-0377) University of Copenhagen Postdoctoral Fellow Bioinformatics The University of Texas Health Science Center at San Antonio Exciting PhD Positions in Modern Biology VBC PhD Programme PhD fellow in Plant Transport Processes University of Copenhagen More Science jobs from Structural basis for the RING-catalyzed synthesis of K63-linked ubiquitin chains   pp597 - 602 Emma Branigan, Anna Plechanovova, Ellis G Jaffray, James H Naismith and Ronald T Hay doi:10.1038/nsmb.3052 Structural analyses capture RING E3 ligase RNF4 bound to Ube2V2-Ubc13 E2 complex charged with ubiquitin and, along with functional assays, reveal the basis for synthesis of K63-linked chains. Recognition of microbial glycans by human intelectin-1   pp603 - 610 Darryl A Wesener, Kittikhun Wangkanont, Ryan McBride, Xuezheng Song, Matthew B Kraft,Heather L Hodges, Lucas C Zarling, Rebecca A Splain, David F Smith, Richard D Cummings, James C Paulson, Katrina T Forest & Laura L Kiessling doi:10.1038/nsmb.3053 Extensive glycan microarray and structural analyses reveal that human intelectin-1 interacts selectively with microbial glycan epitopes through recognition of a terminal 1,2-diol group, an interaction that would be blocked in human glycans such as α-Neu5Ac. SR protein kinases promote splicing of nonconsensus introns   pp611 - 617 Jesse J Lipp, Michael C Marvin, Kevan M Shokat and Christine Guthrie doi:10.1038/nsmb.3057 Chemical genetics, proteomics and biochemistry are used to probe the functions of SR protein kinases. An identified target of Dsk1 is spliceosomal protein Bpb1 (SF1), whose phosphorylation increased its binding to introns with nonconsensus splice sites. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks   pp618 - 626 Hongda Huang, Caroline B Strømme, Giulia Saredi, Martina Hödl, Anne Strandsby,Cristina González-Aguilera, Shoudeng Chen, Anja Groth & Dinshaw J Patel doi:10.1038/nsmb.3055 Chromatin reassembly after replication requires recycling of old and deposition of new histones. Structural insights into how MCM2, part of the replicative helicase, interacts with H3-H4 suggest a function in histone recycling at replication forks. See also: News and Views by Clement & Almouzni Structure of human ST8SiaIII sialyltransferase provides insight into cell-surface polysialylation   pp627 - 635 Gesa Volkers, Liam J Worrall, David H Kwan, Ching-Ching Yu, Lars Baumann,Emilie Lameignere, Gregory A Wasney, Nichollas E Scott, Warren Wakarchuk, Leonard J Foster, Stephen G Withers & Natalie C J Strynadka doi:10.1038/nsmb.3060 Structural studies of human polysialyltransferase ST8SialII in apo form and in complex with donor sugar and sulfated glycan acceptor shed light on the substrate binding and specificity as well as the catalytic activity of this class of polysialyltransferases. Substrate-modulated ADP/ATP-transporter dynamics revealed by NMR relaxation dispersion   pp636 - 641 Sven Brüschweiler, Qin Yang, Changqing Run and James J Chou doi:10.1038/nsmb.3059 NMR relaxation dispersion measurements reveal the conformational dynamics of the mitochondrial ADP/ATP carrier and show that the ADP substrate facilitates interconversion between the predominant cytosol-facing state and a sparsely populated excited state. Brief Communication Top The molecular basis for flexibility in the flexible filamentous plant viruses   pp642 - 644 Frank DiMaio, Chun-Chieh Chen, Xiong Yu, Brandon Frenz, Yau-Heiu Hsu,Na-Sheng Lin & Edward H Egelman doi:10.1038/nsmb.3054 Flexible filamentous plant viruses, which cause substantial crop damage worldwide, have eluded structural characterization so far. The cryo-EM structure of BaMV now reveals the virus architecture and the structural basis of its flexibility. Corrigendum Top Corrigendum: The zinc-finger domains of PARP1 cooperate to recognize DNA strand breaks   p645 Ammar A E Ali, Gyula Timinszky, Raquel Arribas-Bosacoma, Marek Kozlowski, Paul O Hassa,Markus Hassler, Andreas G Ladurner, Laurence H Pearl & Antony W Oliver doi:10.1038/nsmb0815-645a 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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