Tuesday, December 8, 2015

Nature Structural & Molecular Biology Contents: 2015 Volume #22 pp 941-1033

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Nature Structural & Molecular Biology

TABLE OF CONTENTS

December 2015 Volume 22, Issue 12

Correspondence
News and Views
Perspective
Articles
Brief Communication
Resource
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Correspondence

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Ligand occupancy in crystal structure of β1-adrenergic G protein-coupled receptor   pp941 - 942
Andrew G W Leslie, Tony Warne and Christopher G Tate
doi:10.1038/nsmb.3130

Ligand occupancy in crystal structure of β1-adrenergic G protein-coupled receptor   p942
Jianyun Huang, Shuai Chen, J Jillian Zhang and Xin-Yun Huang
doi:10.1038/nsmb.3131

News and Views

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Q&A: repeat-containing proteins   pp943 - 945
Regina M Murphy
doi:10.1038/nsmb.3135
Polyglutamine (polyGln) expansions induce protein misfolding and aggregation into fibrillar deposits, which are believed to underlie forms of neurodegeneration through a mechanism involving gain of toxic function. Polyalalanine expansions are now shown to differ from polyGln in kinetics of aggregation, morphology of aggregates and mechanism of toxicity.

See also: Article by Polling et al.

Src defines a new pool of EGFR substrates   pp945 - 947
Nicole Michael and Natalia Jura
doi:10.1038/nsmb.3137
The mechanisms guiding the substrate specificity of kinases are still poorly understood. Two recent reports provide further insights into how the epidermal growth factor receptor (EGFR) tyrosine kinase recognizes targets by identifying a new consensus motif that requires a Src-mediated priming phosphorylation.

See also: Article by Begley et al.

Replication- and transcription-independent histone exchange in oocytes   p947
Katrina Woolcock
doi:10.1038/nsmb.3143

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Perspective

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Probing molecular choreography through single-molecule biochemistry   pp948 - 952
Antoine M van Oijen and Nicholas E Dixon
doi:10.1038/nsmb.3119
In this Perspective, the authors discuss how recent innovations in single-molecule fluorescence approaches now permit protein dynamics to be monitored in increasingly complex biological systems and cellular environments.

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Articles

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Structure of full-length human anti-PD1 therapeutic IgG4 antibody pembrolizumab   pp953 - 958
Giovanna Scapin, Xiaoyu Yang, Winifred W Prosise, Mark McCoy, Paul Reichert, Jennifer M Johnston, Ramesh S Kashi & Corey Strickland
doi:10.1038/nsmb.3129
IgG4 antibodies can exchange Fab arms and show different affinities for Fc receptors than do other IgG subclasses. The structure of full-length pembrolizumab, a human IgG4 approved to treat advanced melanoma, provides a framework to understand IgG4's properties.

A new vertebrate SUMO enzyme family reveals insights into SUMO-chain assembly   pp959 - 967
Nathalie Eisenhardt, Viduth K Chaugule, Stefanie Koidl, Mathias Droescher, Esen Dogan, Jan Rettich, Päivi Sutinen, Susumu Y Imanishi, Kay Hofmann, Jorma J Palvimo & Andrea Pichler
doi:10.1038/nsmb.3114
The SUMO E3 ligase ZNF451 is a representative member of a new class of SUMO enzymes that execute catalysis via tandem SUMO-interaction motifs, thus allowing efficient SUMO-chain formation.

Structural basis for catalytic activation by the human ZNF451 SUMO E3 ligase   pp968 - 975
Laurent Cappadocia, Andrea Pichler and Christopher D Lima
doi:10.1038/nsmb.3116
Structural and biochemical analyses establish the catalytic mechanism of ZNF451, a new class of E3 ligases.

The architecture of a eukaryotic replisome   pp976 - 982
Jingchuan Sun, Yi Shi, Roxana E Georgescu, Zuanning Yuan, Brian T Chait, Huilin Li & Michael E O'Donnell
doi:10.1038/nsmb.3113
Single-particle electron microscopy reconstruction of the budding yeast replisome locates leading-strand Pol ε and lagging-strand Pol α on opposite sides of the CMG helicase and suggests a new DNA path through the complex during replication.

EGF-receptor specificity for phosphotyrosine-primed substrates provides signal integration with Src   pp983 - 990
Michael J Begley, Cai-hong Yun, Christina A Gewinner, John M Asara, Jared L Johnson, Anthony J Coyle, Michael J Eck, Irina Apostolou & Lewis C Cantley
doi:10.1038/nsmb.3117
Preference of EGFR for substrates that are primed by prior phosphorylation provides the molecular explanation for integration of Src and EGFR signaling via Src-mediated phosphorylation of the adaptor protein Shc1.

See also: News and Views by Michael & Jura

The role of lipids in mechanosensation   pp991 - 998
Christos Pliotas, A Caroline E Dahl, Tim Rasmussen, Kozhinjampara R Mahendran, Terry K Smith, Phedra Marius, Joseph Gault, Thandiwe Banda, Akiko Rasmussen, Samantha Miller, Carol V Robinson, Hagan Bayley, Mark S P Sansom, Ian R Booth & James H Naismith
doi:10.1038/nsmb.3120
Crystallographic, biophysical and in silico analyses indicate that the conformational state of the mechanosensitive channel MscS is determined by the reorganization, due to changes in membrane tension, of the lipids within and around the protein.

R loops regulate promoter-proximal chromatin architecture and cellular differentiation   pp999 - 1007
Poshen B Chen, Hsiuyi V Chen, Diwash Acharya, Oliver J Rando and Thomas G Fazzio
doi:10.1038/nsmb.3122
New data show that R loops differentially modulate binding of chromatin remodelers Tip60-p400 and PRC2 at coding and noncoding gene promoters of mouse ESCs and thereby control transcription and cellular differentiation.

Polyalanine expansions drive a shift into α-helical clusters without amyloid-fibril formation   pp1008 - 1015
Saskia Polling, Angelique R Ormsby, Rebecca J Wood, Kristie Lee, Cheryl Shoubridge, James N Hughes, Paul Q Thomas, Michael D W Griffin, Andrew F Hill, Quill Bowden, Till Böcking & Danny M Hatters
doi:10.1038/nsmb.3127
In vitro and in vivo analyses show that the aggregation mechanism of polyalanine expansions is based on assembly into α-helical clusters with diverse oligomeric species, in contrast to that of polyglutamine expansions, which form amyloid fibrils.

See also: News and Views by Murphy

Structural characterization of human heparanase reveals insights into substrate recognition   pp1016 - 1022
Liang Wu, Cristina M Viola, Andrzej M Brzozowski and Gideon J Davies
doi:10.1038/nsmb.3136
Crystal structures of human heparanase in its apo form and bound to oligosaccharide substrates offer insights into the mechanism of substrate recognition and catalysis.

Brief Communication

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The Tetrahymena telomerase p75-p45-p19 subcomplex is a unique CST complex   pp1023 - 1026
Bingbing Wan, Ting Tang, Heather Upton, Jin Shuai, Yuanzhe Zhou, Song Li, Juan Chen, Joseph S Brunzelle, Zhixiong Zeng, Kathleen Collins, Jian Wu & Ming Lei
doi:10.1038/nsmb.3126
New crystal structures and supporting functional assays identify the p19 and p45 subunits of Tetrahymena telomerase as homologs of the Stn1 and Ten1 subunits of the CST complex, which coordinates telomere replication.

Resource

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Conserved mRNA-binding proteomes in eukaryotic organisms   pp1027 - 1033
Ana M Matiá-Gonzalez, Emma E Laing and André P Gerber
doi:10.1038/nsmb.3128
Comprehensive identification of mRNA-binding proteins in S. cerevisiae and C. elegans reveals their evolutionary conservation; strikingly, most components of the glycolytic pathway and proteasome are detected, thus possibly indicating an ancient mechanism for metabolic control.

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