Nature Structural & Molecular Biology Contents: 2014 Volume #21 pp 945-1045

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TABLE OF CONTENTS November 2014 Volume 21, Issue 11 News and Views Perspective Articles Brief Communication Subscribe   Facebook   RSS   Recommend to library   Twitter   Advertisement Nature has once again been ranked the N0.1 weekly science journal with an Impact Factor of 42.351*. Subscribe to Nature for only $42, £42 or €42. You will receive print, online and app access, providing unbelievable value for money. This is a limited time offer - so don't miss out and subscribe today! *2013 Journal Citation Reports® (Thomson Reuters, 2014)     News and Views Top An expanding universe of mRNA modifications   pp945 - 946 Samie R Jaffrey doi:10.1038/nsmb.2911 The fate of an mRNA is regulated by internal base modifications that generate the modified nucleotides N6-methyladenosine, 5-methylcytosine and inosine. Three new studies show that yeast and human mRNAs also contain pseudouridine residues and that pseudouridylation is induced in various stress states, hinting at a new pathway for post-transcriptional control of mRNA. PARP1 and CBP lose their footing in cancer   pp947 - 948 Gyula Timinszky and Andreas G Ladurner doi:10.1038/nsmb.2913 The human histone macroH2A.1.1 recruits activated PARP1 enzyme to chromatin through its poly(ADP-ribose)-binding macrodomain. New work shows that PARP1 and CBP can be displaced from chromatin in cancer cells that have lost macroH2A.1.1, thus leading to changes in histone H2B acetylation at cancer-relevant genes. See also: Article by Chen et al. Perspective DNA methylation: old dog, new tricks?   pp949 - 954 Cornelia G Spruijt and Michiel Vermeulen doi:10.1038/nsmb.2910 Emerging evidence from genome-wide analyses reveals that DNA methylation, an epigenetic modification associated with the repression of gene expression, can also promote transcriptional activation. Structural & Molecular Biology JOBS of the week Four-Year Science PhD Studentships Institute of Cancer Research (ICR) 2 Technical Assistant Positions (BTA / MTA / CTA) Charité - Universitätsmedizin Berlin - MKFZ Assistant / Associate Professor (Job 14479) University of Missouri - Kansas City Postdoctral Fellow in Molecular Simulation Field Molecular Modeling and Simulation Group, JAEA Postdoctoral Fellow Harvard Medical School More Science jobs from Structural & Molecular Biology EVENT Advances & Progress in Drug Design 16.02.15 london, UK More science events from Articles Top Cross-talking noncoding RNAs contribute to cell-specific neurodegeneration in SCA7   pp955 - 961 Jennifer Y Tan, Keith W Vance, Miguel A Varela, Tamara Sirey, Lauren M Watson et al. doi:10.1038/nsmb.2902 CAG-repeat expansion in the housekeeping gene ATXN7 causes the neurodegenerative disorder SCA7. Now ATXN7 protein is found to promote transcription and expression of miR-124, which in turn mediates cross-talk between lnc-SCA7 and ATXN7 transcripts. Structure and mechanism of action of the BRCA2 breast cancer tumor suppressor   pp962 - 968 Taha Shahid, Joanna Soroka, Eric H Kong, Laurent Malivert, Michael J McIlwraith et al. doi:10.1038/nsmb.2899 Structural and biochemical analyses of full-length human BRCA2 reveal how it facilitates RAD51-mediated homologous recombination to repair DNA double-strand breaks. A genome-wide map of adeno-associated virus–mediated human gene targeting   pp969 - 975 David R Deyle, R Scott Hansen, Anda M Cornea, Li B Li, Amber A Burt et al. doi:10.1038/nsmb.2895 A genome-wide screen of gene targeting by an adeno-associated virus vector in human cells reveals that target sites are preferentially located where transcription occurs in the opposite direction from DNA replication, suggesting that colliding polymerases promote homologous recombination. Crystal structures of free and antagonist-bound states of human α9 nicotinic receptor extracellular domain   pp976 - 980 Marios Zouridakis, Petros Giastas, Eleftherios Zarkadas, Dafni Chroni-Tzartou, Piotr Bregestovski et al. doi:10.1038/nsmb.2900 Crystal structures of the extracellular domain of human nAChR, in its apo form and with antagonists methyllycaconitine or α-bungarotoxin bound, are presented. The structures provide insight into the channel-opening mechanism of nAChRs and their pharmacological properties. MacroH2A1.1 and PARP-1 cooperate to regulate transcription by promoting CBP-mediated H2B acetylation   pp981 - 989 Hongshan Chen, Penelope D Ruiz, Leonid Novikov, Alyssa D Casill, Jong Woo Park et al. doi:10.1038/nsmb.2903 Histone variant macroH2A1 represses gene expression in heterochromatin. New data show that it can also stimulate transcription by cooperating with PARP-1 to promote CBP-mediated H2B acetylation and that this regulatory function is lost in cancer cells. See also: News and Views by Timinszky & Ladurner Crystal structure of a SLC11 (NRAMP) transporter reveals the basis for transition-metal ion transport   pp990 - 996 Ines A Ehrnstorfer, Eric R Geertsma, Els Pardon, Jan Steyaert and Raimund Dutzler doi:10.1038/nsmb.2904 The X-ray crystal structure of ScaDMT, a bacterial member of the solute carrier 11 transporter family, identifies conserved residues within the substrate-binding site that confer metal-ion selectivity. Mechanisms for U2AF to define 3′ splice sites and regulate alternative splicing in the human genome   pp997 - 1005 Changwei Shao, Bo Yang, Tongbin Wu, Jie Huang, Peng Tang et al. doi:10.1038/nsmb.2906 U2AF is known to affect 3′-splice-site selection. Here, Fu and colleagues use genome-wide analysis of U2AF-RNA interactions to define U2AF's key roles in gene expression and regulated splicing in normal and disease states. A mechanism for intracellular release of Na+ by neurotransmitter/sodium symporters   pp1006 - 1012 Lina Malinauskaite, Matthias Quick, Linda Reinhard, Joseph A Lyons, Hideaki Yano et al. doi:10.1038/nsmb.2894 Crystal structures of MhsT, a bacterial member of the neurotransmitter/sodium symporter family, in an occluded, inward-facing state with bound sodium and substrate reveal conformational changes during the transport cycle that provide new insights into the mechanism of cytoplasmic sodium release. Brief Communication Top Crystal structure of the vitamin B3 transporter PnuC, a full-length SWEET homolog   pp1013 - 1015 Michael Jaehme, Albert Guskov and Dirk Jan Slotboom doi:10.1038/nsmb.2909 An X-ray crystal structure of substrate-bound Neisseria PnuC, a bacterial member of the SWEET family of transporters, provides key insights into the translocation mechanism and potential evolution of these membrane proteins. 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