Advertisement |  | Academy of Military Medical Sciences - Celebrating 60 years of research at one of China's leading organizations for medical science.
The Academy of Military Medical Sciences (AMMS) in Beijing has developed beyond its military heritage to become a world leader in medical science with a string of achievements in both military and civilian applications that have resonated around the globe. Find out more about the AMMS in Part 3 of the five-part series of this special sponsor feature on nature.com. |  |
| |  | TABLE OF CONTENTS
| May 2012 Volume 19, Issue 5 |  | | |  |  News and Views
Research Highlights
Articles
Brief Communication
| | | | | | | Advertisement | | 
Nature Outlook: Multiple Sclerosis
Nature Outlook: Multiple sclerosis covers the latest research into how MS starts, and explores new ways to diagnose and treat it.
Access the Outlook online. |
| | | | News and Views |  Top | |  | | Enforcing silencing: dynamic HP1 complexes in Neurospora pp465 - 467
Lori L Wallrath and Sarah C R Elgin
doi:10.1038/nsmb.2291
Abstract | Full Text | PDF
See also: Article by Honda et al.
| | | | Dynein dynamics pp467 - 469
Peter Höök and Richard Vallee
doi:10.1038/nsmb.2290
Abstract | Full Text | PDF
See also: Article by Schmidt et al.
| | Research Highlights | | | | Understanding decoding | Small RNA-mediated DNA repair | Un-arrested development | Mad1 attachment
| Articles | | | | Heterochromatin protein 1 forms distinct complexes to direct histone deacetylation and DNA methylation pp471 - 477
Shinji Honda, Zachary A Lewis, Kenji Shimada, Wolfgang Fischle, Ragna Sack and Eric U Selker
doi:10.1038/nsmb.2274
Methylated histone H3 Lys9 is a hallmark of heterochromatin, and directs DNA methylation via a complex containing heterochromatin protein 1 (HP1) and a DNA methyltransferase. Genetic and biochemical studies in Neurospora now identify a distinct HP1 complex containing a histone deacetylase that is required for silencing independently of DNA methylation, suggesting that distinct HP1 complexes function in parallel to assemble silent heterochromatin.
Abstract | Full Text | PDF
See also: News and Views by Wallrath & Elgin
| | | | p53-mediated heterochromatin reorganization regulates its cell fate decisions pp478 - 484
Sathish Kumar Mungamuri, Erica Kay Benson, Shaomeng Wang, Wei Gu, Sam W Lee and Stuart A Aaronson
doi:10.1038/nsmb.2271
SUV39H1 is a histone methyltransferase responsible for the repressive H3K9me3 mark. New data indicate that SUV39H1, via p21, is a target of p53 repression, leading to decreased H3K9me3 levels at p53 promoters and facilitating p53 activation of its target genes.
Abstract | Full Text | PDF
| | | |
| | |
| | Structure of the c10 ring of the yeast mitochondrial ATP synthase in the open conformation pp485 - 491
Jindrich Symersky, Vijayakanth Pagadala, Daniel Osowski, Alexander Krah, Thomas Meier, José D Faraldo-Gómez and David M Mueller
doi:10.1038/nsmb.2284
The membrane-embedded c-ring allows the passage of protons to power the synthesis of ATP by the FoF1 ATPase. Previous structural data have shown the proton acceptor-donor sites in a closed, ion-locked conformation. Structural and computational data now reveal the open conformation of the yeast mitochondrial c10 ring.
Abstract | Full Text | PDF
| | | | Insights into dynein motor domain function from a 3.3-Å crystal structure pp492 - 497
Helgo Schmidt, Emma S Gleave and Andrew P Carter
doi:10.1038/nsmb.2272
Dynein is a molecular motor involved in many cellular functions. The motor domain of dynein contains six AAA+ domains forming a ring that interacts with the motile linker domain. The structure of yeast dynein motor domain crystallized without nucleotides is now presented at 3.3-Å resolution and shows the specific contacts between linker and ring, with nucleotide interactions at the different AAA+ domains revealed by soaking experiments.
Abstract | Full Text | PDF
See also: News and Views by Höök & Vallee
| | | | The cryo-EM structure of the UPF–EJC complex shows UPF1 poised toward the RNA 3′ end pp498 - 505
Roberto Melero, Gretel Buchwald, Raquel Castaño, Monika Raabe, David Gil, Melisa Lázaro, Henning Urlaub, Elena Conti and Oscar Llorca
doi:10.1038/nsmb.2287
The nonsense-mediated mRNA decay (NMD) pathway is triggered upon assembly of the UPF surveillance complex near an exon junction complex (EJC). Cryo-EM studies have revealed the geometry of this transient assembly between the UPF complex and the EJC, which demonstrates how the UPF1 subunit elicits its RNA helicase activity toward the 3A end of the mRNA.
Abstract | Full Text | PDF
| | | | Discovery of an archetypal protein transport system in bacterial outer membranes pp506 - 510
Joel Selkrig, Khedidja Mosbahi, Chaille T Webb, Matthew J Belousoff, Andrew J Perry, Timothy J Wells, Faye Morris, Denisse L Leyton, Makrina Totsika, Minh-Duy Phan, Nermin Celik, Michelle Kelly, Clare Oates, Elizabeth L Hartland, Roy M Robins-Browne, Sri Harsha Ramarathinam, Anthony W Purcell, Mark A Schembri, Richard A Strugnell, Ian R Henderson, Daniel Walker and Trevor Lithgow
doi:10.1038/nsmb.2261
Bacterial secretion systems are key to pathogenesis, as they secrete the many virulence factors needed for host colonization. Bioinformatic and functional analyses have identified a transport and assembly module (TAM) in proteobacteria that may be necessary for biogenesis of the autotransporter family of virulence factors.
Abstract | Full Text | PDF
| | | | NEDD8 links cullin-RING ubiquitin ligase function to the p97 pathway pp511 - 516
Willem den Besten, Rati Verma, Gary Kleiger, Robert S Oania and Raymond J Deshaies
doi:10.1038/nsmb.2269
The AAA+ protein p97 and its UBA-UBX cofactors are thought to promote degradation by separating ubiquitinated proteins from membranes or protein complexes. UBA-UBX proteins can interact with cullin-RING ubiquitin ligases, and UBXD7 is now seen to specifically bind NEDD8 on active, neddylated cullins, promoting degradation of a Cul3 substrate.
Abstract | Full Text | PDF
| | | | Human prion protein binds Argonaute and promotes accumulation of microRNA effector complexes pp517 - 524
Derrick Gibbings, Pascal Leblanc, Florence Jay, Dominique Pontier, Fabrice Michel, Yannick Schwab, Sandrine Alais, Thierry Lagrange and Olivier Voinnet
doi:10.1038/nsmb.2273
The association of Argonaute (Ago) proteins with endomembranes is thought to be important for their function. New analyses now demonstrate that a transmembrane form of human prion protein binds Ago through GW-motif-containing octarepeat domains and promotes the accumulation of miRISC effector complexes, thereby mediating effective repression of miRNA targets.
Abstract | Full Text | PDF
| | | | Synergistic substrate binding determines the stoichiometry of transport of a prokaryotic H+/Cl− exchanger pp525 - 531
Alessandra Picollo, Yanyan Xu, Niklaus Johner, Simon Bernèche and Alessio Accardi
doi:10.1038/nsmb.2277
Mechanistic studies of active exchangers suggest that substrate binding in active exchangers is antagonistic, and coupling is maintained by preventing shuttling of the empty transporter. However, isothermal titration calorimetry and free energy calculations now show that substrate binding of H+ and Cl− to the prokaryotic CLC-ec1 exchanger is synergistic and occurs simultaneously.
Abstract | Full Text | PDF
| | | | Antidiabetic phospholipid–nuclear receptor complex reveals the mechanism for phospholipid-driven gene regulation pp532 - 537
Paul M Musille, Manish C Pathak, Janelle L Lauer, William H Hudson, Patrick R Griffin and Eric A Ortlund
doi:10.1038/nsmb.2279
Liver receptor homolog 1 (LHR-1) is a nuclear receptor involved in development, lipid homeostasis and metabolism. The crystal structures of the LHR-1 ligand-binding domain in its apo state and in complex with the phospholipid DLPC are now presented. The data, along with biophysical and functional analyses, reveal the highly dynamic nature of the apo receptor and show how DLPC binding affects co-regulator selectivity.
Abstract | Full Text | PDF
| | | | ATP binding controls distinct structural transitions of Escherichia coli DNA gyrase in complex with DNA pp538 - 546
Aakash Basu, Allyn J Schoeffler, James M Berger and Zev Bryant
doi:10.1038/nsmb.2278
Bacterial DNA gyrase uses the energy from ATP to introduce negative supercoils into DNA via formation of a chiral wrap intermediate. Now DNA rotation and contraction are simultaneously visualized using a single-molecule setup. The data reveal multiple steps, including a dominant non-chiral intermediate step.
Abstract | Full Text | PDF
| | | | Rapid oligomer formation of human muscle acylphosphatase induced by heparan sulfate pp547 - 554
Neda Motamedi-Shad, Tommaso Garfagnini, Amanda Penco, Annalisa Relini, Federico Fogolari, Alessandra Corazza, Gennaro Esposito, Francesco Bemporad and Fabrizio Chiti
doi:10.1038/nsmb.2286
Heparan sulfate can promote formation of amyloid fibrils by different proteins. The early steps and kinetics of this process are now studied in detail, using a stopped-flow setup and the protein mAcP. The data and analysis reveal two steps, binding of mAcP to heparan sulfate and conversion to a misfolded state, followed by aggregation of the heparan sulfate–bound proteins.
Abstract | Full Text | PDF
| | Brief Communication | Top | | | | Crystal structure of a group II intron in the pre-catalytic state pp555 - 557
Russell T Chan, Aaron R Robart, Kanagalaghatta R Rajashankar, Anna Marie Pyle and Navtej Toor
doi:10.1038/nsmb.2270
Group II introns, which are self-splicing catalytic RNAs, catalyze splicing in two distinct steps. The crystal structure of a group II intron in the pre-catalytic state directly preceding the first splicing step reveals a sharp kink in the backbone that presents the scissile phosphate of the splice site to the active site.
First paragraph | Full Text | PDF
| | | Top | | | | Advertisement | | Nature Reviews Molecular Cell Biology
FOCUS ON METABOLISM
Cells rapidly adapt to changes in nutrient availability and integrate this information about their metabolic state to drive cellular processes. Unprecedented insights are being gained into the molecular basis of how metabolic pathways interface with cell biological processes and how this can be disrupted in metabolic disorders.
Read the Focus online at:
www.nature.com/nrm/focus/metabolism |
|
| | | | | | | | | | 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 | | | | | |
| |
|
No comments:
Post a Comment