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| April 2012 Volume 19, Issue 4 |  | | |  |  News and Views
Research Highlights
Review
Articles
Brief Communications
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| | | | News and Views |  Top | |  | | | | Articles | Top | | | | The structure of the ASAP core complex reveals the existence of a Pinin-containing PSAP complex pp378 - 386
Andrea Giovanni Murachelli, Judith Ebert, Claire Basquin, Hervé Le Hir and Elena Conti
doi:10.1038/nsmb.2242
The ASAP complex is emerging as an assembly of proteins at the interface between transcription, pre-mRNA splicing and mRNA quality control. Structural analysis of the ASAP core complex reveals macromolecular interactions between the subunits and their assembly into ASAP. In addition, ASAP subunits SAP18 and RNPS1 are shown to bind Pinin, forming a novel complex called PSAP.
Abstract | Full Text | PDF
| | | | A telomere-dependent DNA damage checkpoint induced by prolonged mitotic arrest pp387 - 394
Makoto T Hayashi, Anthony J Cesare, James A J Fitzpatrick, Eros Lazzerini-Denchi and Jan Karlseder
doi:10.1038/nsmb.2245
Mammalian telomeres are protected by shelterin components to avoid being recognized as DNA damage. Now cells under prolonged mitotic arrest are found to deprotect their telomeres, with dissociation of shelterin subunit TRF2 and degradation of the G-strand overhang. This leads to DNA damage signaling and checkpoint activation and apoptosis in the following G1 phase.
Abstract | Full Text | PDF
| | | | Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation pp395 - 402
Michael Hohl, Christophe Briand, Markus G Grütter and Markus A Seeger
doi:10.1038/nsmb.2267
TM287/288 is a heterodimeric ABC transporter found in Thermotoga maritima. The crystal structure of TM287/288 in the inward-facing AMP-PNP–bound state provides new insight into nucleotide binding by heterodimeric transporters and will serve as an important model for eukaryotic disease-associated homologs.
Abstract | Full Text | PDF
| | | | A conserved proline switch on the ribosome facilitates the recruitment and binding of trGTPases pp403 - 410
Li Wang, Fang Yang, Dejiu Zhang, Zhi Chen, Rui-Ming Xu, Knud H Nierhaus, Weimin Gong and Yan Qin
doi:10.1038/nsmb.2254
Recruitment of elongation factor EF-G to the ribosome requires interaction between ribosomal proteins L12 and L11. New analyses identify a proline switch in L11, with the cis configuration allowing direct interaction between L11 and L12. EF-G has peptidyl-prolyl cis-trans isomerase activity driving the cis-trans isomerization of the proline switch, which might be a universal mechanism for efficient turnover of translational GTPases.
Abstract | Full Text | PDF
| | | | Diverse HIV viruses are targeted by a conformationally dynamic antiviral pp411 - 416
Matthew E C Caines, Katsiaryna Bichel, Amanda J Price, William A McEwan, Greg J Towers, Brian J Willett, Stefan M V Freund and Leo C James
doi:10.1038/nsmb.2253
Rhesus macaque TRIMCyp (RhTC) is a potent antiviral that inhibits the replication of diverse HIV viruses. New studies reveal that RhTC has evolved to become conformationally dynamic, and that RhTC can be engineered to switch from a single conformation that can target only HIV-1 to a dynamic state that can target multiple viral strains.
Abstract | Full Text | PDF
| | | | Topoisomerase I poisoning results in PARP-mediated replication fork reversal pp417 - 423
Arnab Ray Chaudhuri, Yoshitami Hashimoto, Raquel Herrador, Kai J Neelsen, Daniele Fachinetti, Rodrigo Bermejo, Andrea Cocito, Vincenzo Costanzo and Massimo Lopes
doi:10.1038/nsmb.2258
Topoisomerase 1 (Top1) inhibition is believed to mediate cellular toxicity by trapping Top1 on nicked DNA, leading to double-strand break formation during replication. New studies show that clinically relevant doses of Top1 poisons lead instead to extensive replication-fork reversal that is mediated by Poly(ADP-ribose) polymerases, limiting double-strand break formation.
Abstract | Full Text | PDF
| | | | A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71 pp424 - 429
Xiangxi Wang, Wei Peng, Jingshan Ren, Zhongyu Hu, Jiwei Xu, Zhiyong Lou, Xumei Li, Weidong Yin, Xinliang Shen, Claudine Porta, Thomas S Walter, Gwyndaf Evans, Danny Axford, Robin Owen, David J Rowlands, Junzhi Wang, David I Stuart, Elizabeth E Fry and Zihe Rao
doi:10.1038/nsmb.2255
Enterovirus 71 (EV71) is a major agent of hand, foot and mouth disease in children, but no vaccine or antiviral therapy is available. Structural analysis of the mature virus and natural empty particles reveals that the larger empty particles resemble elusive enterovirus uncoating intermediates, allowing insight into the process of enterovirus uncoating.
Abstract | Full Text | PDF
See also: News and Views by Hogle
| | | | Structure of N-terminal domain of ZAP indicates how a zinc-finger protein recognizes complex RNA pp430 - 435
Shoudeng Chen, Yihui Xu, Kuo Zhang, Xinlu Wang, Jian Sun, Guangxia Gao and Yingfang Liu
doi:10.1038/nsmb.2243
Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses such as HIV-1 by targeting viral mRNA for degradation. Structural analysis now reveals a large RNA-binding surface comprising many positively charged residues and two cavities, thereby providing insight into how ZAP recognizes its target RNA.
Abstract | Full Text | PDF
| | | | The molecular architecture of human Dicer pp436 - 440
Pick-Wei Lau, Keelan Z Guiley, Nabanita De, Clinton S Potter, Bridget Carragher and Ian J MacRae
doi:10.1038/nsmb.2268
Current understanding of the structure of Dicer is restricted to simple forms of the enzyme from lower eukaryotes or isolated domains from higher eukaryotic Dicers. A new domain localization strategy was developed to determine the structure of human Dicer by EM, revealing the structural basis for small RNA production in eukaryotes.
Abstract | Full Text | PDF
See also: News and Views by Sawh & Duchaine
| | | | Control of RNP motility and localization by a splicing-dependent structure in oskar mRNA pp441 - 449
Sanjay Ghosh, Virginie Marchand, Imre Gáspár and Anne Ephrussi
doi:10.1038/nsmb.2257
oskar mRNA localization to the posterior pole of the Drosophila melanogaster oocyte requires splicing of the first intron and the exon junction complex (EJC). In vitro and in vivo analyses demonstrate that splicing has a dual role in oskar mRNA localization by generating a secondary structural element required for RNP motility and depositing the EJC required for mRNA transport.
Abstract | Full Text | PDF
| | | | Structure of the ternary initiation complex aIF2–GDPNP–methionylated initiator tRNA pp450 - 454
Emmanuelle Schmitt, Michel Panvert, Christine Lazennec-Schurdevin, Pierre-Damien Coureux, Javier Perez, Andrew Thompson and Yves Mechulam
doi:10.1038/nsmb.2259
Archaeal initiation factor 2 (aIF2) in its GTP-bound form binds methionylated initiator tRNA to form a ternary initiation complex. Its 3D structure, as determined by crystallography and small-angle X-ray scattering analysis, reveals that despite the structural homology between aIF2 and elongation factor EF1A, these two G proteins of the translation apparatus use very different tRNA-binding strategies.
Abstract | Full Text | PDF
| | Brief Communications | Top | | | | Structure of the activating IL-1 receptor signaling complex pp455 - 457
Christoph Thomas, J Fernando Bazan and K Christopher Garcia
doi:10.1038/nsmb.2260
Interleukin-1 (IL-1) cytokines are important mediators of the innate and adaptive immune response. The structure of IL-1β bound to its receptor (IL-IR) and receptor accessory protein (IL-1RAcP) provides an important model for how these cytokines initiate signaling.
First paragraph | Full Text | PDF
| | | | The SUMO protease SENP7 is a critical component to ensure HP1 enrichment at pericentric heterochromatin pp458 - 460
Christèle Maison, Kelly Romeo, Delphine Bailly, Marion Dubarry, Jean-Pierre Quivy and Geneviève Almouzni
doi:10.1038/nsmb.2244
SUMOylation targets HP1α to pericentric heterochromatin, but the enzyme responsible for removing the SUMO molecule from HP1a has not been determined. SENP7 is now identified as the factor that deconjugates SUMO, promoting retention of HP1α at these domains.
First paragraph | Full Text | PDF
| | | | Structure of the human metapneumovirus fusion protein with neutralizing antibody identifies a pneumovirus antigenic site pp461 - 463
Xiaolin Wen, Jens C Krause, George P Leser, Reagan G Cox, Robert A Lamb, John V Williams, James E Crowe Jr and Theodore S Jardetzky
doi:10.1038/nsmb.2250
The crystal structure of the fusion protein from human metapneumovirus in complex with a potently neutralizing antibody reveals a novel antigenic site, which could be explored to develop vaccines against this and related paramyxoviruses.
First paragraph | Full Text | PDF
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