Tuesday, June 7, 2016

Nature Structural & Molecular Biology Contents: 2016 Volume #23 pp 463-618

If you are unable to see the message below, click here to view.
Nature Structural & Molecular Biology

TABLE OF CONTENTS

June 2016 Volume 23, Issue 6

Focus
Editorial
Commentary
Perspectives
Reviews
Obituary
News and Views
Articles
Resource
Subscribe
 
Facebook
 
RSS
 
Recommend to library
 
Twitter
 

Focus

Top
Focus on Membrane Proteins
Focus issue: June 2016 Volume 23 No 6

Editorial

Top

Focus on Membrane Proteins
Cellular gatekeepers   p463
doi:10.1038/nsmb.3246
In a common yet effective analogy, a cell can be compared to a fortified city, in which lipid membranes form the defensive walls, and membrane proteins function as gates and checkpoints that control the transit of molecules and information across these walls. We evoke this concept on the cover of this special Focus on Membrane Proteins.

Commentary

Top

Focus on Membrane Proteins
Atomic-level analysis of membrane-protein structure   pp464 - 467
Wayne A Hendrickson
doi:10.1038/nsmb.3215
Wayne Hendrickson discusses the consortium efforts and developments in methodology that in recent years have allowed unprecedented advances in atomic-structure determination of membrane proteins.

Perspectives

Top

Focus on Membrane Proteins
NMR as a tool to investigate the structure, dynamics and function of membrane proteins   pp468 - 474
Binyong Liang and Lukas K Tamm
doi:10.1038/nsmb.3226
This Perspective provides an overview of recent progress, successes, challenges and future opportunities in the application of solution NMR and solid-state NMR methods to study the structure, dynamics and function of membrane proteins.

Focus on Membrane Proteins
Toward high-resolution computational design of the structure and function of helical membrane proteins   pp475 - 480
Patrick Barth and Alessandro Senes
doi:10.1038/nsmb.3231
This Perspective provides an overview of the major advances in recent years in the computational design and structure prediction of α-helical membrane proteins.

Focus on Membrane Proteins
Nanodiscs for structural and functional studies of membrane proteins   pp481 - 486
Ilia G Denisov and Stephen G Sligar
doi:10.1038/nsmb.3195
The use of nanodiscs is substantially fostering structural and functional studies of membrane protein. This Perspective summarizes the recent use of nanodiscs as an invaluable tool for the characterization of membrane proteins.

Reviews

Top

Focus on Membrane Proteins
Mechanistic diversity in ATP-binding cassette (ABC) transporters   pp487 - 493
Kaspar P Locher
doi:10.1038/nsmb.3216
ABC transporters use ATP hydrolysis to translocate substrates across cell membranes. Kaspar Locher reviews the mechanistic diversity of ABC transporters, as has emerged from recent structural studies, and discusses future directions for investigation of ABC-transporter-catalyzed reactions.

Focus on Membrane Proteins
Structural mechanisms of activation and desensitization in neurotransmitter-gated ion channels   pp494 - 502
Andrew J R Plested
doi:10.1038/nsmb.3214
Numerous recent crystal and cryo-EM structures have greatly advanced understanding of the functional mechanisms of neurotransmitter-gated ion channels. This Review discusses the structural basis of activation and desensitization mechanisms in glutamate and cysteine-loop receptors.

Obituary

Top

Knud Hermann Nierhaus 1941-2016   pp503 - 504
Daniel N Wilson and Christian M T Spahn
doi:10.1038/nsmb.3239

News and Views

Top

Escape from epigenetic silencing of lactase expression is triggered by a single-nucleotide change   pp505 - 507
Dallas M Swallow and Jesper T Troelsen
doi:10.1038/nsmb.3238
The importance of subtle gene regulation and epigenetics in determining complex human traits is increasingly being recognized. However, bridging the gaps between environmental, epigenetic and genetic influences and unraveling causal relationships remain a big challenge. A study now reports an example of epigenetic changes influenced by genetic factors that are involved in the regulation of lactase gene expression.

See also: Article by Labrie et al.

Reverse transcriptases lend a hand in splicing catalysis   pp507 - 509
Joseph A Piccirilli and Jonathan P Staley
doi:10.1038/nsmb.3242
The first high-resolution views of group II intron maturases illuminate the architectural and functional roles of these multidomain proteins in splicing and DNA invasion. The maturases show striking structural and functional homology to a central protein involved in spliceosomal pre-messenger RNA splicing, thus reinforcing the idea that group II introns and the spliceosome descended from a common ancestor.

See also: Article by Qu et al. | Article by Zhao & Pyle

Noncoding RNA joins Ku and DNA-PKcs for DNA-break resistance in breast cancer   pp509 - 510
Susan P Lees-Miller, Tara L Beattie and John A Tainer
doi:10.1038/nsmb.3240
The noncoding RNA LINP1 acts as a scaffold that links Ku and DNA-PKcs and enables efficient DNA double-strand-break repair through nonhomologous end joining (NHEJ), thereby enhancing the resistance of triple-negative breast cancer cells to radiation and chemotherapies.

See also: Article by Zhang et al.

Heavy lessons in protein allostery   pp511 - 512
Lars Konermann
doi:10.1038/nsmb.3234
Hydrogen/deuterium exchange mass spectrometry reveals that the antiapoptotic protein MCL-1 is inhibited by a covalent modification far from its functional site. This finding opens new avenues for cancer therapy, but it also highlights that much remains to be learned about the fundamental basis of allosteric regulation.

See also: Article by Lee et al.

Structural & Molecular Biology
JOBS of the week
Research Fellow in Structural Molecular Virology
University of Leeds
Postdoctoral Position in Chemical Biology of Tubulin Modifications : Lausanne, Switzerland
EPFL Swiss Federal Institute of Technology Lausanne


IGBMC call for Group Leader positions
IGBMC
Exciting PhD Positions in Modern Biology
VBC PhD Programme
More Science jobs from
Structural & Molecular Biology
EVENT
Lipid-protein interactions and organelle function
01.09.16
Spetses, Greece
More science events from

Articles

Top

Crystal structure of the prefusion surface glycoprotein of the prototypic arenavirus LCMV   pp513 - 521
Kathryn M Hastie, Sebastien Igonet, Brian M Sullivan, Pierre Legrand, Michelle A Zandonatti et al.
doi:10.1038/nsmb.3210
The crystal structure of the GP1-GP2 complex of the prototypical arenavirus LCMV in prefusion form sheds light on the conformational changes that the arenavirus glycoprotein undergoes to cause fusion.

Long noncoding RNA LINP1 regulates repair of DNA double-strand breaks in triple-negative breast cancer   pp522 - 530
Youyou Zhang, Qun He, Zhongyi Hu, Yi Feng, Lingling Fan et al.
doi:10.1038/nsmb.3211
New data reveal that LINP1, a lncRNA overexpressed in triple-negative breast cancer, interacts with the Ku70-Ku80 complex and DNA-PKcs, thereby promoting NHEJ-mediated DNA double-strand-break repair.

See also: News and Views by Lees-Miller et al.

Extensive subunit contacts underpin herpesvirus capsid stability and interior-to-exterior allostery   pp531 - 539
Alexis Huet, Alexander M Makhov, Jamie B Huffman, Matthijn Vos, Fred L Homa et al.
doi:10.1038/nsmb.3212
Capsids from two herpesviruses (HSV-1 and PRV), imaged inside intact virions, are analyzed by cryo-EM. The maps allowed the construction of a complete model of subunit and domain organization, revealing extensive subunit contacts.

BRD4 is a histone acetyltransferase that evicts nucleosomes from chromatin   pp540 - 548
Ballachanda N Devaiah, Chanelle Case-Borden, Anne Gegonne, Chih Hao Hsu, Qingrong Chen et al.
doi:10.1038/nsmb.3228
In vitro and in vivo analyses show that BRD4 has intrinsic acetyltransferase activity targeting histones H3 and H4, and BRD4 acetylation of H3 K122 results in histone eviction, nucleosome clearance and chromatin decompaction.

Structure of a group II intron in complex with its reverse transcriptase   pp549 - 557
Guosheng Qu, Prem Singh Kaushal, Jia Wang, Hideki Shigematsu, Carol Lyn Piazza et al.
doi:10.1038/nsmb.3220
A 3.8-A cryo-EM structure of a bacterial group IIA intron in complex with its intron-encoded protein reveals how the reverse transcriptase domain interacts with the mobile intron RNA as well as structural similarities with eukaryotic telomerase and spliceosomal components.

See also: News and Views by Piccirilli & Staley | Article by Zhao & Pyle

Crystal structures of a group II intron maturase reveal a missing link in spliceosome evolution   pp558 - 565
Chen Zhao and Anna Marie Pyle
doi:10.1038/nsmb.3224
Crystal structures of the reverse transcriptase domains of two group II intron-encoded proteins reveal their similarity to the RT domain of splicing factor Prp8, thus suggesting a common ancestry shared by group II introns and the spliceosome.

See also: News and Views by Piccirilli & Staley | Article by Qu et al.

Lactase nonpersistence is directed by DNA-variation-dependent epigenetic aging   pp566 - 573
Viviane Labrie, Orion J Buske, Edward Oh, Richie Jeremian, Carolyn Ptak et al.
doi:10.1038/nsmb.3227
Age-dependent epigenetic changes that are influenced by genetic factors contribute to lactase nonpersistence, which is linked to the inability of adult mammals to digest lactose.

See also: News and Views by Swallow & Troelsen

Structure of the Dcp2-Dcp1 mRNA-decapping complex in the activated conformation   pp574 - 579
Eugene Valkov, Sowndarya Muthukumar, Chung-Te Chang, Stefanie Jonas, Oliver Weichenrieder et al.
doi:10.1038/nsmb.3232
Crystal structures, along with biochemistry data, capture the active form of the Dcp2 decapping enzyme in complex with Dcp1 and a peptide from Edc1, thus revealing the mechanism of activation by Dcp1 and Edc1 activators.

Functional interplay between MSL1 and CDK7 controls RNA polymerase II Ser5 phosphorylation   pp580 - 589
Sarantis Chlamydas, Herbert Holz, Maria Samata, Tomasz Chelmicki, Plamen Georgiev et al.
doi:10.1038/nsmb.3233
MSL1, a component of the Drosophila dosage compensation complex, genetically and biochemically interacts with CDK7, a subunit of the TFIIH transcription factor, thus revealing a complex interplay between MSL1 and the general transcriptional machinery.

Mechanism of extracellular ion exchange and binding-site occlusion in a sodium/calcium exchanger   pp590 - 599
Jun Liao, Fabrizio Marinelli, Changkeun Lee, Yihe Huang, Jose D Faraldo-Gomez et al.
doi:10.1038/nsmb.3230
A series of crystal structures and calculated free-energy landscapes of a Na+/Ca2+ exchanger explain how its alternating-access mechanism is controlled by the ion occupancy, thus leading to coupled antiport.

Allosteric inhibition of antiapoptotic MCL-1   pp600 - 607
Susan Lee, Thomas E Wales, Silvia Escudero, Daniel T Cohen, James Luccarelli et al.
doi:10.1038/nsmb.3223
Identification of an allosteric mechanism disrupting the antiapoptotic BH3 binding activity of MCL-1 offers a new approach for targeting the apoptotic resistance of human cancers.

See also: News and Views by Konermann

Resource

Top

Multilayered proteomics reveals molecular switches dictating ligand-dependent EGFR trafficking   pp608 - 618
Chiara Francavilla, Moreno Papetti, Kristoffer T G Rigbolt, Anna-Kathrine Pedersen, Jon O Sigurdsson et al.
doi:10.1038/nsmb.3218
Analysis of changes in the EGFR interactome, ubiquitinome, phosphoproteome and proteome in response to EGF or TGF-α identifies RAB7 phosphorylation and RCP recruitment to EGFR as ligand-specific switches controlling receptor trafficking, signal duration and cellular responses.

Top
nature events
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

You have been sent this Table of Contents Alert because you have opted in to receive it. You can change or discontinue your e-mail alerts at any time, by modifying your preferences on your nature.com account at: www.nature.com/myaccount
(You will need to log in to be recognised as a nature.com registrant)

For further technical assistance, please contact our registration department

For print subscription enquiries, please contact our subscription department

For other enquiries, please contact our customer feedback department

Nature Publishing Group | One New York Plaza, Suite 4500 | New York | NY 10004-1562 | USA

Nature Publishing Group's worldwide offices:
London - Paris - Munich - New Delhi - Tokyo - Melbourne
San Diego - San Francisco - Washington - New York - Boston

Macmillan Publishers Limited is a company incorporated in England and Wales under company number 785998 and whose registered office is located at The Campus, 4 Crinan Street, London, N1 9XW.

© 2016 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.

nature publishing group

No comments: