Tuesday, May 6, 2014

Nature Structural & Molecular Biology Contents: 2014 Volume #21 pp 289-425

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Nature Structural & Molecular Biology
TABLE OF CONTENTS

May 2014 Volume 21, Issue 5

Obituary
News and Views
Articles
Brief Communication

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Nature Structural & Molecular Biology 
FOCUS ON UBIQUITIN 

Ubiquitin and ubiquitin-like proteins have central roles in regulating cellular processes and homeostasis. This Focus examines our understanding of the ubiquitination reaction and the mechanisms by which ubiquitin and related modifications affect key cellular functions.

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Obituary

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Iain D Campbell 1941-2014   pp427 - 428
Christina Redfield
doi:10.1038/nsmb.2821

News and Views

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How T cells taste gluten in celiac disease   pp429 - 431
Bana Jabri, Xi Chen and Ludvig M Sollid
doi:10.1038/nsmb.2826
Genome-wide association studies have identified genes encoding major histocompatibility (MHC) class II molecules as the single most important predisposing factor for autoimmunity. A new study provides atomic insight into how the antigen receptors of intestinal T cells recognize dietary gluten that drives celiac disease pathogenesis when bound to the MHC class II molecule HLA-DQ2.5, the major genetic risk factor of celiac disease.

See also: Article by Petersen et al.

JAK-cytokine receptor recognition, unboxed   pp431 - 433
Randall McNally and Michael J Eck
doi:10.1038/nsmb.2824
The crystal structure of the FERM-SH2 region of Tyk2 in complex with the cytoplasmic tail of an interferon-α receptor provides a first view of specific JAK-receptor recognition and reveals a central role of the heretofore-marginalized JAK SH2 domain in recognizing the cytokine-receptor box2 motif.

See also: Article by Wallweber et al.

Let it go: how to deal with a breakup in mitosis   pp433 - 435
Eros Lazzerini Denchi and Julia Li
doi:10.1038/nsmb.2825
A new report reveals how mammalian cells silence the DNA-damage response during mitosis to allow cell division to be completed in the presence of DNA lesions.

How YidC inserts and folds proteins across a membrane   pp435 - 436
Ross E Dalbey and Andreas Kuhn
doi:10.1038/nsmb.2823
The crystal structure of the membrane insertase YidC reveals a hydrophilic groove in the cytoplasmic bilayer leaflet, suggesting a new mechanism of membrane-protein insertion.

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Articles

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Crystal structure of ATP-bound Get3–Get4–Get5 complex reveals regulation of Get3 by Get4   pp437 - 442
Harry B Gristick, Meera Rao, Justin W Chartron, Michael E Rome, Shu-ou Shan et al.
doi:10.1038/nsmb.2813
Tail-anchor proteins are targeted post-translationally to the endoplasmic reticulum via the conserved GET pathway, in which the Get4–Get5 complex mediates delivery of substrates to Get3, the central targeting factor. The crystal structure of the ATP-bound Get3–Get4–Get5 complex and functional analyses reveal how Get4–Get5 primes Get3 for substrate loading.

Structural basis of recognition of interferon-a receptor by tyrosine kinase 2   pp443 - 448
Heidi J A Wallweber, Christine Tam, Yvonne Franke, Melissa A Starovasnik and Patrick J Lupardus
doi:10.1038/nsmb.2807
How the four JAK kinases discriminate between different cytokine receptors is not well understood. The first crystal structure of a JAK kinase (TYK2) bound to a cytokine receptor (INFAR1) now exposes a multipoint interaction mode that involves an atypical phosphoindependent interaction between TYK2's SH2 domain and INFAR1's conserved box2 motif.

See also: News and Views by McNally & Eck

Kin28 regulates the transient association of Mediator with core promoters   pp449 - 455
Célia Jeronimo and François Robert
doi:10.1038/nsmb.2810
The genomic localization of Mediator in budding yeast is now assessed, revealing that Mediator remains associated with upstream activating sequences until it becomes transiently associated with core promoters during initiation. Phosphorylation of the CTD of Rpb1 at Ser5 by Kin28 releases Mediator prior to elongation.

Conformational changes required for H+/Cl exchange mediated by a CLC transporter   pp456 - 463
Daniel Basilio, Kristin Noack, Alessandra Picollo and Alessio Accardi
doi:10.1038/nsmb.2814
CLC-type H+/Cl exchangers are known to be regulated by voltage and H+ and Clconcentrations, but their gating mechanism remains poorly understood. New data now suggest that transport by the CLCs is regulated by two gates that are functionally linked through structural rearrangements outside of the ion-transport pathway.

Evidence for a group II intron–like catalytic triplex in the spliceosome   pp464 - 471
Sebastian M Fica, Melissa A Mefford, Joseph A Piccirilli and Jonathan P Staley
doi:10.1038/nsmb.2815
It has long been thought that the catalytic RNAs of self-splicing group II introns and the spliceosome function by similar mechanisms. Now, a combination of genetic, cross-linking, and biochemical analyses of yeast U6 snRNA provide compelling evidence that spliceosomal RNAs form triplex structures similar to those used by group II introns to catalyze splicing.

Conformational dynamics of ligand-dependent alternating access in LeuT   pp472 - 479
Kelli Kazmier, Shruti Sharma, Matthias Quick, Shahidul M Islam, Benoît Roux et al.
doi:10.1038/nsmb.2816
LeuT is a Na+-coupled amino acid transporter that is similar in sequence and function to eukaryotic neurotransmitter/sodium symporters, which are active in reuptake of neurotransmitters from the synapse. Distance measurements between spin-label pairs are used to identify ligand-dependent structural transitions in LeuT.

T-cell receptor recognition of HLA-DQ2–gliadin complexes associated with celiac disease   pp480 - 488
Jan Petersen, Veronica Montserrat, Jorge R Mujico, Khai Lee Loh, Dennis X Beringer et al.
doi:10.1038/nsmb.2817
A central event in celiac disease (CD) is the recognition by TCRs of gluten epitopes presented by specific HLAs, with HLA-DQ2 being associated with 95% of CD cases. The molecular basis for these interactions are now revealed by crystal structures of TCRs from individuals with CD in complex with wheat gliadin epitopes presented by HLA-DQ2.

See also: News and Views by Jabri et al.

Mechanism of activation of bacterial cellulose synthase by cyclic di-GMP   pp489 - 496
Jacob L W Morgan, Joshua T McNamara and Jochen Zimmer
doi:10.1038/nsmb.2803
Cyclic di-GMP (c-di-GMP) regulates a number of bacterial processes, including synthesis of cellulose during biofilm formation. The PilZ domain from bacterial cellulose synthase BcsA–BcsB senses c-di-GMP and activates the enzyme. Now crystal structures of BcsA–BcsB along with functional analysis reveal that binding of c-di-GMP releases a conserved gating loop to allow substrate to enter the active site.

Brief Communication

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Role of polymerase β in complementing aprataxin deficiency during abasic-site base excision repair   pp497 - 499
Melike Çaglayan, Vinod K Batra, Akira Sassa, Rajendra Prasad and Samuel H Wilson
doi:10.1038/nsmb.2818
5'-adenylated DNA adducts generated during nucleotide excision repair (NER) are removed by aprataxin to permit DNA end ligation. Now, structural and kinetic analyses reveal that NER enzymes DNA polymerase β and FEN1 can also excise these adducts and thus provide a 'backup' repair pathway for abasic sites.

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