TABLE OF CONTENTS
| June 2012 Volume 19, Issue 6 |  | | |  |  Focus
Editorial
Reviews
Perspective
Research Highlights
Articles
Brief Communications
| | | | | | | 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 |
| | | | Focus |  Top | |  | | | | Translational Control |  | Focus issue: June 2012 Volume 19 No 6 |
| | Editorial | Top | | | | Focus on Translational Control
Translational control decrypted p559
doi:10.1038/nsmb.2321
Recent research efforts have made great strides in elucidating the process, machinery and mechanisms that control how mRNAs are decoded by ribosomes in the process of protein translation.
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| | Reviews | Top | | | | Focus on Translational Control
One core, two shells: bacterial and eukaryotic ribosomes pp560 - 567
Sergey Melnikov, Adam Ben-Shem, Nicolas Garreau de Loubresse, Lasse Jenner, Gulnara Yusupova and Marat Yusupov
doi:10.1038/nsmb.2313
The recent X-ray structures of the complete ribosome and large and small subunits from eukaryotes allow these structures to be compared to the previously determined structures of bacterial ribosomes. This Review describes bacterial and eukaryotic ribosomes as a conserved core and two specific shells and focuses on selected bacteria- and eukaryote-specific structural features and their functional implications.
Abstract | Full Text | PDF
| | | | Focus on Translational Control
A mechanistic overview of translation initiation in eukaryotes pp568 - 576
Colin Echeverría Aitken and Jon R Lorsch
doi:10.1038/nsmb.2303
Translation initiation requires the formation of a pre-initiation complex that recruits the 5A end of the mRNA and scans along it to locate the start codon. Genetic, biochemical and structural studies have shed light on the molecular mechanisms underlying the individual steps of this complex process. This Review describes our current understanding of eukaryotic translation initiation and outlines some important outstanding questions in the field.
Abstract | Full Text | PDF
| | | | Focus on Translational Control
Translational control by changes in poly(A) tail length: recycling mRNAs pp577 - 585
Laure Weill, Eulàlia Belloc, Felice-Alessio Bava and Raúl Méndez
doi:10.1038/nsmb.2311
Recent studies have revealed how poly(A) tail length and the selection of alternative polyadenylation sites contribute to translational control. This Review discusses how mechanisms of alternative polyadenylation, deadenylation and cytoplasmic polyadenylation are coordinated to modulate gene expression in inflammation, learning and memory acquisition, and early development.
Abstract | Full Text | PDF
| | | | Focus on Translational Control
The mechanics of miRNA-mediated gene silencing: a look under the hood of miRISC pp586 - 593
Marc R Fabian and Nahum Sonenberg
doi:10.1038/nsmb.2296
Understanding how microRNAs (miRNAs) silence targeted mRNAs has been the focus of intensive research. This Review describes recent advances, with an emphasis on how the miRNA-mediated silencing complex (miRISC) controls gene expression by inhibiting translation and/or mRNA decay, and how trans-acting factors control miRNA action.
Abstract | Full Text | PDF
| | Perspective | | | | Focus on Translational Control
Translation drives mRNA quality control pp594 - 601
Christopher J Shoemaker and Rachel Green
doi:10.1038/nsmb.2301
Cells have evolved so-called mRNA surveillance mechanisms to monitor mRNAs as they are translated and to degrade troublesome transcripts. Studies of mRNA surveillance have traditionally focused on mRNA fate. In this Perspective, the authors explore mRNA surveillance from the viewpoint of its origins on the ribosome, which should lead to new and unanticipated insights that inform future studies.
Abstract | Full Text | PDF
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| Research Highlights | Top | | | | Focus on Translational Control
APA regulator | Translational control of viral infection | Translation under hypoxia
| Articles | Top | | | | PABP and the poly(A) tail augment microRNA repression by facilitated miRISC binding pp603 - 608
Francesca Moretti, Constanze Kaiser, Agnieszka Zdanowicz-Specht and Matthias W Hentze
doi:10.1038/nsmb.2309
Although the poly(A) tail and poly(A) binding protein (PABP) have emerged as important effectors of miRNA function, how they contribute to miRNA-mediated gene silencing has been unclear. A combination of biochemical and functional studies now demonstrate that PABP promotes the association of miRISC with its target mRNAs.
Abstract | Full Text | PDF
| | | | Real-time assembly landscape of bacterial 30S translation initiation complex pp609 - 615
Pohl Milón, Cristina Maracci, Liudmila Filonava, Claudio O Gualerzi and Marina V Rodnina
doi:10.1038/nsmb.2285
Translation initiation proceeds in several steps, and one of the early events involves the binding of three initiation factors, mRNA and initiator tRNA to the 30S ribosomal subunit, which is known as the 30S pre-initiation complex (PIC) assembly. Systematic FRET studies now uncover the kinetically favored assembly pathway of the 30S PIC.
Abstract | Full Text | PDF
| | | | Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine pp616 - 622
Steven E Glynn, Andrew R Nager, Tania A Baker and Robert T Sauer
doi:10.1038/nsmb.2288
A biochemical study reveals the AAA+ protein unfoldase ClpX functions as a closed ring and identifies regions required for intersubunit coupling during the ATPase cycle. These findings provide important insights on the ClpX mechanism that may be extended to other AAA+ proteins.
Abstract | Full Text | PDF
| | | | A rule of seven in Watson-Crick base-pairing of mismatched sequences pp623 - 627
Ibrahim I Cisse, Hajin Kim and Taekjip Ha
doi:10.1038/nsmb.2294
Sequence recognition through base pairing is essential for DNA repair and gene regulation, but the basic rules underlying this process have been unclear. Data from single-molecule fluorescence studies, used to visualize annealing and melting reactions of two untethered strands containing a single mismatch, suggest that seven contiguous base pairs are needed for rapid annealing of DNA and RNA.
Abstract | Full Text | PDF
| | | | Structural basis for cisplatin DNA damage tolerance by human polymerase η during cancer chemotherapy pp628 - 632
Ajay Ummat, Olga Rechkoblit, Rinku Jain, Jayati Roy Choudhury, Robert E Johnson, Timothy D Silverstein, Angeliki Buku, Samer Lone, Louise Prakash, Satya Prakash and Aneel K Aggarwal
doi:10.1038/nsmb.2295
Cisplatin forms intrastrand cross-links on DNA and is a widely used chemotherapy agent. Among human translesion DNA polymerases, Pol-η can bypass cisplatin adducts. The crystal structure of human Pol-η in complex with a DNA template with a cisplatin lesion is now presented. In addition to the larger active site, the structure reveals specific interactions with the adduct by residues that are not conserved in other translesion polymerases.
Abstract | Full Text | PDF
| | | | A glutamate switch controls voltage-sensitive phosphatase function pp633 - 641
Lijun Liu, Susy C Kohout, Qiang Xu, Simone Müller, Christopher R Kimberlin, Ehud Y Isacoff and Daniel L Minor Jr
doi:10.1038/nsmb.2289
The voltage-sensing domain of Ci-VSP regulates the enzymatic activity of its PTEN-like phosphatase domain. New structural and functional data identify a gating loop that controls access to the enzyme's active site and is coupled to voltage sensor movements.
Abstract | Full Text | PDF
| | | | A locally closed conformation of a bacterial pentameric proton-gated ion channel pp642 - 649
Marie S Prevost, Ludovic Sauguet, Hugues Nury, Catherine Van Renterghem, Christèle Huon, Frederic Poitevin, Marc Baaden, Marc Delarue and Pierre-Jean Corringer
doi:10.1038/nsmb.2307
Pentameric ligand-gated ion channels (pLGICs) mediate fast synaptic signaling in response to neurotransmitter binding, but the conformational changes induced by neurotransmitter binding are unknown. The crystal structures of mutated GLIC, a bacterial pLGIC homolog, reveal a novel, locally closed channel conformation that provides insight into pLGIC allosteric transitions.
Abstract | Full Text | PDF
| | Brief Communications | Top | | | | Efficiency and specificity in microRNA biogenesis pp650 - 652
Omer Barad, Mati Mann, Elik Chapnik, Archana Shenoy, Robert Blelloch, Naama Barkai and Eran Hornstein
doi:10.1038/nsmb.2293
Primary microRNA cleavage by the Microprocessor complex comprising Drosha and DGCR8 needs to be specific yet efficient. Mathematical modeling complemented with experimental analysis now shows that autoregulatory feedback on DGCR8 expression is crucial for balancing the efficiency and specificity of Microprocessor activity.
First paragraph | Full Text | PDF
| | | | Structure of mammalian poly(ADP-ribose) glycohydrolase reveals a flexible tyrosine clasp as a substrate-binding element pp653 - 656
In-Kwon Kim, James R Kiefer, Chris M W Ho, Roderick A Stegeman, Scott Classen, John A Tainer and Tom Ellenberger
doi:10.1038/nsmb.2305
Poly ADP-ribosylation regulates cellular processes such as genomic stability maintenance, transcription and cell death. The structure of a mammalian poly(ADP-ribose) glycohydrolase gives insight into the enzyme's endoglycosidase activity and provides a basis for the development of therapeutic inhibitors.
First paragraph | Full Text | PDF
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