Wednesday, May 6, 2015

Nature Structural & Molecular Biology Contents: 2015 Volume #22 pp 349-431

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Nature Structural & Molecular Biology

TABLE OF CONTENTS

May 2015 Volume 22, Issue 5

Correspondence
News and Views
Research Highlights
Articles
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Correspondence

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Say it with proteins: an alphabet of crystal structures   p349
Mark Howarth
doi:10.1038/nsmb.3011

News and Views

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A little less leads to lots more   pp350 - 351
Jonathan R Warner
doi:10.1038/nsmb.3023
Mammalian cells have both cytoplasmic and mitochondrial ribosomes, which have long been considered to operate completely independently. However, a new report shows that after heat shock, MRPL18, a human mitochondrial ribosomal protein, binds to cytoplasmic ribosomes to influence translation of heat-shock mRNAs.

See also: Article by Zhang et al.

Light-driven Na+ pumps as next-generation inhibitory optogenetic tools   pp351 - 353
Przemyslaw Nogly and Jorg Standfuss
doi:10.1038/nsmb.3017
The first structures of a light-driven sodium pump provide insight into the mechanism of ion transport and selectivity. Genetic manipulation of rat neuronal cells and of Caenorhabditis elegans worms demonstrates the utility of such pumps for optogenetic applications.

See also: Article by Gushchin et al.

A bumpy road for RNA polymerase II   pp353 - 355
Luciana E Giono and Alberto R Kornblihtt
doi:10.1038/nsmb.3020
The identification of a second regulatory checkpoint controlling RNA polymerase II elongation near the poly(A) site of protein-coding genes reveals an additional level of complexity in the modulation of eukaryotic transcriptional elongation and termination.

See also: Article by Laitem et al.

Integrin bondage: filamin takes control   pp355 - 357
Nicola De Franceschi and Johanna Ivaska
doi:10.1038/nsmb.3024
Regulation of integrin activity is critical for human health, and the steps mediating integrin activation are well established. In contrast, the counteracting mechanisms of inactivation are less understood. An integrin inhibitor, filamin, is shown to stabilize the integrin resting state by bondage of the cytoplasmic domains of the integrin heterodimer, thus providing evidence of a new mechanism for integrin retention in the inactive state.

See also: Article by Liu et al.

A molecular syringe that kills cells   pp357 - 359
Elena V Orlova
doi:10.1038/nsmb.3021
R-type pyocins, produced by Pseudomonas aeruginosa, are sheath-tube nanomachines that puncture the envelopes of target cells, inducing their death. Cryo-EM studies reveal the atomic structures of the pyocin R2 in its extended precontraction and postcontraction forms, which suggest a mechanism for the contraction process of this molecular syringe.

See also: Article by Ge et al.

Dynactin revealed   pp359 - 360
Samara L Reck-Peterson
doi:10.1038/nsmb.3022
Dynactin is an essential cofactor for the microtubule-based motor cytoplasmic dynein. Two recent papers report structures obtained by cryo-EM of dynactin, the dynein-dynactin complex and dynein-dynactin bound to its track, the microtubule.

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Research Highlights

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A barrier-breaking resolution | The yin and yang of eIF3 | Mammalian mitoribosomes revealed | SETX attenuates antiviral transcription

Articles

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PRESTO-Tango as an open-source resource for interrogation of the druggable human GPCRome   pp362 - 369
Wesley K Kroeze, Maria F Sassano, Xi-Ping Huang, Katherine Lansu, John D McCorvy et al.
doi:10.1038/nsmb.3014
Roth and colleagues have developed PRESTO-Tango, a new open-source platform for high-throughput screening of the entire human nonolfactory GPCRome, and they show how it can be used to identify new ligands for orphan human GPCRs.

A lncRNA regulates alternative splicing via establishment of a splicing-specific chromatin signature   pp370 - 376
Inma Gonzalez, Roberto Munita, Eneritz Agirre, Travis A Dittmer, Katia Gysling et al.
doi:10.1038/nsmb.3005
The evolutionarily conserved antisense long noncoding RNA asFGFR2 influences cell type–specific alternative-splicing patterns of FGFR2 by recruiting chromatin modifiers to the locus.

Atomic structures of a bactericidal contractile nanotube in its pre- and postcontraction states   pp377 - 382
Peng Ge, Dean Scholl, Petr G Leiman, Xuekui Yu, Jeff F Miller et al.
doi:10.1038/nsmb.2995
Cryo-EM structures of the pre- and postcontraction states of Pseudomonas aeruginosa R-type pyocins provide details of the conformational changes between the tube and sheath that take place during contraction.

See also: News and Views by Orlova

Structural mechanism of integrin inactivation by filamin   pp383 - 389
Jianmin Liu, Mitali Das, Jun Yang, Sujay Subbayya Ithychanda, Valentin P Yakubenko et al.
doi:10.1038/nsmb.2999
The integrin inhibitor filamin competes with activators for integrin binding, but an NMR structural analysis now reveals that filamin also functions by stabilizing integrin in its resting state.

See also: News and Views by De Franceschi & Ivaska

Crystal structure of a light-driven sodium pump   pp390 - 395
Ivan Gushchin, Vitaly Shevchenko, Vitaly Polovinkin, Kirill Kovalev, Alexey Alekseev et al.
doi:10.1038/nsmb.3002
Crystal structures of the microbial rhodopsin KR2, a recently discovered light-driven sodium pump, reveal the translocation pathway of sodium ions and shed light on the molecular mechanism of ion pumping.

See also: News and Views by Nogly & Standfuss

CDK9 inhibitors define elongation checkpoints at both ends of RNA polymerase II–transcribed genes   pp396 - 403
Clélia Laitem, Justyna Zaborowska, Nur F Isa, Johann Kufs, Martin Dienstbier et al.
doi:10.1038/nsmb.3000
Genome-wide mapping of CDK9-dependent transcription-elongation checkpoints reveals an unexpected control point near the poly(A) site of pol II–transcribed human genes.

See also: News and Views by Giono & Kornblihtt

Translational control of the cytosolic stress response by mitochondrial ribosomal protein L18   pp404 - 410
Xingqian Zhang, Xiangwei Gao, Ryan Alex Coots, Crystal S Conn, Botao Liu et al.
doi:10.1038/nsmb.3010
A stress-induced cytosolic isoform of the mitochondrial ribosomal protein MRPL18 facilitates the specific translation of heat-shock proteins during the general shutdown of protein synthesis that occurs in response to cellular stress.

See also: News and Views by Warner

Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX   pp411 - 416
Benjamin M Stinson, Vladimir Baytshtok, Karl R Schmitz, Tania A Baker and Robert T Sauer
doi:10.1038/nsmb.3012
The hexameric ClpX AAA+ ATPase requires subunit asymmetry and switching between nucleotide-loadable and nucleotide-unloadable conformations for cooperative ATP hydrolysis and efficient substrate binding, unfolding and degradation.

Notch is a direct negative regulator of the DNA-damage response   pp417 - 424
Jelena Vermezovic, Marek Adamowicz, Libero Santarpia, Alessandra Rustighi, Mattia Forcato et al.
doi:10.1038/nsmb.3013
Assays in both C. elegans and human cells show that Notch interacts with ATM kinase to inhibit the DNA-damage response and that Notch activity is inversely correlated with ATM activation in breast cancer cells.

Atomic structure of the Y complex of the nuclear pore   pp425 - 431
Kotaro Kelley, Kevin E Knockenhauer, Greg Kabachinski and Thomas U Schwartz
doi:10.1038/nsmb.2998
Solving the crystal structure of the Y-complex hub allowed Schwartz and colleagues to assemble a high-resolution composite structure of the complete Y complex, one of the principal nuclear pore complex scaffolds.

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