Wednesday, March 4, 2015

Nature Structural & Molecular Biology Contents: 2015 Volume #22 pp 175-272

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Nature Structural & Molecular Biology

TABLE OF CONTENTS

March 2015 Volume 22, Issue 3

Editorial
News and Views
Research Highlights
Articles
Brief Communications
Corrigenda
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Editorial

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Announcement: double-blind peer review   p175
doi:10.1038/nsmb.2983
Nature and Nature Research Journals start offering anonymity to authors during the peer-review process.

News and Views

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Ribonucleotides in DNA: hidden in plain sight   pp176 - 178
Sue Jinks-Robertson and Hannah L Klein
doi:10.1038/nsmb.2981
Mapping of ribonucleotides to single-nucleotide resolution in yeast genomes provides new insight into the enzymology of DNA replication.

See also: Article by Clausen et al. | Article by Daigaku et al.

Subversive bacteria reveal new tricks in their cytoskeleton-hijacking arsenal   pp178 - 179
Roberto Dominguez
doi:10.1038/nsmb.2976
During infection, pathogenic Yersinia species secrete the antiphagocytic factor YopO (or YpkA), which contains a kinase domain and a Rho GTPase guanine nucleotide-dissociation inhibitor (GDI) domain. The structure of YopO in complex with actin, along with biochemical analyses, reveals the mechanism by which YopO uses actin to activate its kinase domain and recruit, phosphorylate and deactivate actin-assembly factors implicated in phagocytic clearance of the bacterium.

See also: Article by Lee et al.

Secondary nucleation wears the BRICHOS in this family   pp180 - 181
Frank A Ferrone
doi:10.1038/nsmb.2980
A chaperone segment provides powerful evidence for the molecular mechanism underlying Alzheimer's disease.

See also: Article by Cohen et al.

The proteasome gets a grip on protein complexity   pp181 - 183
Matthew A Humbard and Michael R Maurizi
doi:10.1038/nsmb.2977
Amyloids escape elimination by the proteasome, and their accumulation and subsequent aggregation contribute to various neurodegenerative conditions. A signature feature of amyloidogenic proteins is extended sequences rich in single amino acids. In this issue, Matouschek and colleagues now show that, to initiate degradation, the proteasome prefers substrates that have disordered regions with complex amino acid composition, thus indicating why it fails to rid the cell of most amyloids.

See also: Article by Fishbain et al.

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Research Highlights

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Released from the chains of death | m6A drives structural changes in RNA | TSPO through the crystal looking glass

Articles

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Tracking replication enzymology in vivo by genome-wide mapping of ribonucleotide incorporation   pp185 - 191
Anders R Clausen, Scott A Lujan, Adam B Burkholder, Clinton D Orebaugh, Jessica S Williams et al.
doi:10.1038/nsmb.2957
HydEn-seq, a new sequencing method that maps the distribution of ribonucleotides misincorporated by low-fidelity DNA polymerases in budding yeast, reveals unexpected strand-specific replication patterns in both nuclear and mitochondrial genomes.

See also: News and Views by Jinks-Robertson & Klein

A global profile of replicative polymerase usage   pp192 - 198
Yasukazu Daigaku, Andrea Keszthelyi, Carolin A Müller, Izumi Miyabe, Tony Brooks et al.
doi:10.1038/nsmb.2962
Genome-wide DNA polymerase usage maps determined in fission yeast, using a new sequencing strategy based on ribonucleotide misincorporation, track the division of labor between replicative polymerases and reveal locations and efficiencies of replication origins.

See also: News and Views by Jinks-Robertson & Klein

Structural basis for amyloidogenic peptide recognition by sorLA   pp199 - 206
Yu Kitago, Masamichi Nagae, Zenzaburo Nakata, Maho Yagi-Utsumi, Shizuka Takagi-Niidome et al.
doi:10.1038/nsmb.2954
The neuronal sorting receptor SorLA protects against Alzheimer's disease by binding Aβ peptides. Three new structures of the Vps10p Aβ-binding domain in ligand-free and ligand-bound forms explain the basis of SorLA peptide recognition.

A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers   pp207 - 213
Samuel I A Cohen, Paolo Arosio, Jenny Presto, Firoz Roshan Kurudenkandy, Henrik Biverstål et al.
doi:10.1038/nsmb.2971
Aβ peptide aggregation is associated with Alzheimer's disease, and Aβ fibrils can catalyze formation of toxic oligomers. Molecular chaperone Brichos binds to the fibril surface, inhibiting the catalytic cycle in vitro, and limits Aβ toxicity.

See also: News and Views by Ferrone

Sequence composition of disordered regions fine-tunes protein half-life   pp214 - 221
Susan Fishbain, Tomonao Inobe, Eitan Israeli, Sreenivas Chavali, Houqing Yu et al.
doi:10.1038/nsmb.2958
The proteasome initiates protein degradation at disordered regions within substrates. The proteasomal sequence preferences for the amino acid composition of these regions identified here affect protein half-life and explain unusual stability trends.

See also: News and Views by Humbard & Maurizi

Structures of CYLD USP with Met1- or Lys63-linked diubiquitin reveal mechanisms for dual specificity   pp222 - 229
Yusuke Sato, Eiji Goto, Yuri Shibata, Yuji Kubota, Atsushi Yamagata et al.
doi:10.1038/nsmb.2970
Tumor-suppressor protein CYLD cleaves linear and Lys63-linked ubiquitin chains. Structures of CYLD USP domain with Met1- and Lys63-linked diubiquitins and biochemical analyses reveal the mechanism for dual specificity and provide insight into tumor-associated mutations.

Mechanism of microhomology-mediated end-joining promoted by human DNA polymerase θ   pp230 - 237
Tatiana Kent, Gurushankar Chandramouly, Shane Michael McDevitt, Ahmet Y Ozdemir and Richard T Pomerantz
doi:10.1038/nsmb.2961
Human DNA Polθ can mediate microhomology-mediated end-joining (MMEJ) of DNA molecules in cells and in vitro. Biochemistry work shows that Polθ promotes formation of DNA synapses and strand annealing, activities that require insertion loop 2.

Crystal structure of a phosphorylation-coupled vitamin C transporter   pp238 - 241
Ping Luo, Xinzhe Yu, Weiguang Wang, Shilong Fan, Xiaochun Li et al.
doi:10.1038/nsmb.2975
Crystal structures of the bacterial vitamin C transporter UlaA, a member of the AG family of the phosphoenolpyruvate-dependent phosphotransferase system, provide insights on binding to ascorbate and its transport across the cell membrane.

DNA interstrand cross-link repair requires replication-fork convergence   pp242 - 247
Jieqiong Zhang, James M Dewar, Magda Budzowska, Anna Motnenko, Martin A Cohn et al.
doi:10.1038/nsmb.2956
New biochemical analyses in Xenopus cell-free extracts show that two replication forks must converge on a DNA interstrand cross-link (ICL) to permit translesion synthesis and repair.

Yersinia effector YopO uses actin as bait to phosphorylate proteins that regulate actin polymerization   pp248 - 255
Wei Lin Lee, Jonathan M Grimes and Robert C Robinson
doi:10.1038/nsmb.2964
The crystal structure of Yersinia enterocolitica kinase YopO in complex with monomeric actin, together with biochemical analyses, reveals that YopO uses actin as bait to disrupt host cytoskeleton function and prevent phagocytosis.

See also: News and Views by Dominguez

Exon-intron circular RNAs regulate transcription in the nucleus   pp256 - 264
Zhaoyong Li, Chuan Huang, Chun Bao, Liang Chen, Mei Lin et al.
doi:10.1038/nsmb.2959
The identification of a new subclass of circular RNAs that are predominantly nuclear and promote transcription of their parental genes reveals a new regulatory function for these noncoding RNAs.

Brief Communications

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Structural basis for bifunctional peptide recognition at human δ-opioid receptor   pp265 - 268
Gustavo Fenalti, Nadia A Zatsepin, Cecilia Betti, Patrick Giguere, Gye Won Han et al.
doi:10.1038/nsmb.2965
Serial femtosecond crystallography of the human δ-opioid receptor in complex with an endomorphin-derived peptide reveals interactions that are important for understanding the pharmacology of opioid peptides and developing analgesics with reduced side effects.

Structure of a Yeast 40S–eIF1–eIF1A–eIF3–eIF3j initiation complex   pp269 - 271
Christopher H S Aylett, Daniel Boehringer, Jan P Erzberger, Tanja Schaefer and Nenad Ban
doi:10.1038/nsmb.2963
A high-resolution cryo-EM structure of yeast eIF3-bound 40S ribosomal subunits reveals the network of interactions between eIF3 subunits.

Corrigenda

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Corrigendum: Structure of EF-G-ribosome complex in a pretranslocation state   p272
Yun Chen, Shu Feng, Veerendra Kumar, Rya Ero and Yong-Gui Gao
doi:10.1038/nsmb0315-272a

Corrigendum: Cross-talking noncoding RNAs contribute to cell-specific neurodegeneration in SCA7   p272
Jennifer Y Tan, Keith W Vance, Miguel A Varela, Tamara Sirey, Lauren M Watson et al.
doi:10.1038/nsmb0315-272b

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