Monday, August 6, 2018

Nature Structural & Molecular Biology Contents: 2018 Volume #25 pp 641 - 744

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

August 2018 Volume 25, Issue 8

News & Views
Articles
Amendments & Corrections
 

News & Views

 

Does RNA secondary structure drive translation or vice versa?    pp641 - 643
Marianne C. Kramer & Brian D. Gregory
doi:10.1038/s41594-018-0100-2

Break-induced replication sparks CGG-repeat instability    pp643 - 644
Madhura Deshpande & Jeannine Gerhardt
doi:10.1038/s41594-018-0103-z

Active state of Parkin    pp644 - 646
François Le Guerroué & Richard J. Youle
doi:10.1038/s41594-018-0101-1

Switching 53BP1 on and off via Tudors    pp646 - 647
Yi Zhang & Tatiana G. Kutateladze
doi:10.1038/s41594-018-0104-y

A new twist on V(D)J recombination    pp648 - 649
Fred Dyda & Phoebe A. Rice
doi:10.1038/s41594-018-0107-8

Structural & Molecular Biology
JOBS of the week
Faculty Positions at Institute of Natural Sciences, Westlake University
Westlake University
IBMS Seeking Assistant / Associate / Full Professor
The Institute of Basic Medical Sciences (IBMS)
Research Assistant for the Sugiyama lab in ShanghaiTech University
ShanghaiTech University
Impact and Evaluation Analyst
Wellcome Sanger Institute
Researcher / postdoc
Swedish University of Agricultural Sciences (SLU)
More Science jobs from
Structural & Molecular Biology
EVENT
10th International Congress on Structural Biology
18.10.18
Helsinki, Finland
More science events from

Articles

 

Identification of Exo1-Msh2 interaction motifs in DNA mismatch repair and new Msh2-binding partners    pp650 - 659
Eva M. Goellner, Christopher D. Putnam, William J. Graham V, Christine M. Rahal, Bin-Zhong Li et al.
doi:10.1038/s41594-018-0092-y

A pair of SHIP box motifs identified within the Exo1 nuclease mediate interactions with Msh2 during DNA mismatch repair and define potential new Msh2-binding partners in yeast and human cells.

 

Structural basis for the regulation of inositol trisphosphate receptors by Ca2+ and IP3    pp660 - 668
Navid Paknejad & Richard K. Hite
doi:10.1038/s41594-018-0089-6

Cryo-EM analyses of human IP3 receptor in different ligand states (apo, with Ca2+ and/or IP3) reveal conformational changes in the cytoplasmic domain and how Ca2+ can regulate channel function.

 

Mechanisms of genetic instability caused by (CGG)n repeats in an experimental mammalian system    pp669 - 676
Artem V. Kononenko, Thomas Ebersole, Karen M. Vasquez & Sergei M. Mirkin
doi:10.1038/s41594-018-0094-9

A new system to analyze the instability of fragile X (CGG)n repeats in mammalian cells suggests that long repeats cause replication fork stalling, resulting in repeat length changes and mutation at a distance via break-induced replication.

 

Analyses of mRNA structure dynamics identify embryonic gene regulatory programs    pp677 - 686
Jean-Denis Beaudoin, Eva Maria Novoa, Charles E. Vejnar, Valeria Yartseva, Carter M. Takacs et al.
doi:10.1038/s41594-018-0091-z

Characterization of mRNA structure during the zebrafish maternal-to-zygotic transition identifies the ribosome as a major RNA structure remodeler in vivo and reveals that structural dynamics can affect gene expression, partly by modulating miRNA activity.

 

RNAs interact with BRD4 to promote enhanced chromatin engagement and transcription activation    pp687 - 697
Homa Rahnamoun, Jihoon Lee, Zhengxi Sun, Hanbin Lu, Kristen M. Ramsey et al.
doi:10.1038/s41594-018-0102-0

Cell-based and in vitro analyses reveal that BRD4 functionally associates with eRNAs and that BRD4 bromodomains, through eRNA interactions, promote BRD4 binding at mutant p53-targeted enhancers to augment enhancer activation and tumor promoting gene expression.

 

Cryo-EM structure of the αvβ8 integrin reveals a mechanism for stabilizing integrin extension    pp698 - 704
Anthony Cormier, Melody G. Campbell, Saburo Ito, Shenping Wu, Jianlong Lou et al.
doi:10.1038/s41594-018-0093-x

The cryo-EM structure of human αvβ8 integrin in the extended-closed conformation shows the headpiece rotating about a flexible αv-knee, suggesting a ligand surveillance mechanism for integrins.

 

Atomic insights into the genesis of cellular filaments by globular proteins    pp705 - 714
Laura McPartland, Danielle M. Heller, David S. Eisenberg, Ann Hochschild & Michael R. Sawaya
doi:10.1038/s41594-018-0096-7

A set of GFP fusions with as few as 12 residues appended to the C terminus is shown to assemble into filaments in E. coli. Crystal structures reveal a mechanism termed ‘runaway domain coupling’ and illustrate how protein filament formation can evolve.

 

Cation trafficking propels RNA hydrolysis    pp715 - 721
Nadine L. Samara & Wei Yang
doi:10.1038/s41594-018-0099-4

Time-resolved X-ray crystal structures of RNA hydrolysis by RNase H1 reveal that cations in addition to the two canonical Mg2+ ions position the reactants in the active site and enable catalysis.

 

Structure of a mitochondrial fission dynamin in the closed conformation    pp722 - 731
Olga Bohuszewicz & Harry H. Low
doi:10.1038/s41594-018-0097-6

The mitochondrial fission dynamin (Dnm1) from an algae is captured in a closed conformation, with the GTPase domain compacted against the stalk. This work indicates that formation of the closed conformation may contribute to membrane fission.

 

DNA melting initiates the RAG catalytic pathway    pp732 - 742
Heng Ru, Wei Mi, Pengfei Zhang, Frederick W. Alt, David G. Schatz et al.
doi:10.1038/s41594-018-0098-5

Cryo-EM structures of the RAG endonuclease in complex with intact DNA substrates reveal that DNA melting is the first step in V(D)J recombination, a mechanism potentially conserved in retroviral integration and DNA transposition.

 

Amendments & Corrections

 

Author Correction: H3K64 trimethylation marks heterochromatin and is dynamically remodeled during developmental reprogramming    p743
Sylvain Daujat, Thomas Weiss, Fabio Mohn, Ulrike C Lange, Céline Ziegler-Birling et al.
doi:10.1038/s41594-018-0090-0

Author Correction: Structure of the core of the type III secretion system export apparatus    p743
Lucas Kuhlen, Patrizia Abrusci, Steven Johnson, Joseph Gault, Justin Deme et al.
doi:10.1038/s41594-018-0095-8

Publisher Correction: Mechanism of parkin activation by phosphorylation    p744
Véronique Sauvé, George Sung, Naoto Soya, Guennadi Kozlov, Nina Blaimschein et al.
doi:10.1038/s41594-018-0105-x

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

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

Springer Nature'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.

Nature is part of Springer Nature. © 2018 Springer Nature Limited. All rights reserved.

Springer Nature

No comments: