Translation articles within Nature

Featured

  • Article |

    ANKRD16 attenuates neurodegeneration induced by a mutation in the editing domain of alanyl tRNA synthetase by directly accepting mis-activated serine from the synthetase before transfer to the tRNA, establishing a new mechanism by which editing defects are prevented.

    • My-Nuong Vo
    • , Markus Terrey
    •  & Susan L. Ackerman

  • Letter |

    Mammalian mitochondria use folate-bound one-carbon units generated by the enzyme SHMT2 to methylate tRNA, and this modification is required for mitochondrial translation and thus oxidative phosphorylation.

    • Raphael J. Morscher
    • , Gregory S. Ducker
    •  & Joshua D. Rabinowitz

  • Article |

    A high-resolution structure of the human ribosome determined by cryo-electron microscopy visualizes numerous RNA modifications that are concentrated at functional sites with an extended shell, and suggests the possibility of designing more specific ribosome-targeting drugs.

    • S. Kundhavai Natchiar
    • , Alexander G. Myasnikov
    •  & Bruno P. Klaholz

  • Review Article |

    A review of the recent developments in reprogramming the genetic code of cells and organisms to include non-canonical amino acids in precisely engineered proteins.

    • Jason W. Chin

  • Analysis |

    The large number of small, similarly sized proteins and the small number of heavy RNA molecules that make up a ribosome reduce the time required for reproduction.

    • Shlomi Reuveni
    • , Måns Ehrenberg
    •  & Johan Paulsson

  • Article |

    Structural ensembles of the 70S ribosome bound to cognate or near-cognate charged tRNAs in complex with EF-Tu illustrate the crucial role of the nucleotide G530 in decoding of mRNA, and demonstrate that translational fidelity results from direct control of GTPase by the decoding centre.

    • Anna B. Loveland
    • , Gabriel Demo
    •  & Andrei A. Korostelev

  • Letter |

    The structure of the bacterial 70S ribosome in complex with ArfA, the release factor RF2, a short non-stop mRNA and a cognate P-site tRNA is presented, revealing how ArfA and RF2 facilitate alternative translation termination of the non-stop ribosomal complex using a stop-codon surrogate mechanism.

    • Chengying Ma
    • , Daisuke Kurita
    •  & Ning Gao

  • Article |

    The structures of several states on the pathway of SelB-mediated delivery of selenocysteine-specific tRNA to the ribosome in Escherichia coli reveal the mechanism of UGA stop codon recoding to selenocysteine and show how codon recognition triggers activation of translational GTPases.

    • Niels Fischer
    • , Piotr Neumann
    •  & Holger Stark

  • Letter |

    Drosophila sechellia, a species closely related to the model species Drosophila melanogaster, bypasses a premature stop codon in neuronal cells to express a functional olfactory receptor protein from an assumed pseudogene template.

    • Lucia L. Prieto-Godino
    • , Raphael Rytz
    •  & Richard Benton

  • Letter |

    Here, the selection of substrates by the protein–RNA complex known as the signal recognition particle (SRP) is investigated in the bacterium Escherichia coli, revealing that the SRP has a strong preference for hydrophobic transmembrane domains of inner membrane proteins.

    • Daniela Schibich
    • , Felix Gloge
    •  & Günter Kramer

  • Letter |

    A translation complex sequencing approach has been developed enabling intermediates of all mRNA-associated processes of translation to be isolated and localized across the transcriptome; the results support longstanding models of initiation and termination and offer new mechanistic insights.

    • Stuart K. Archer
    • , Nikolay E. Shirokikh
    •  & Thomas Preiss

  • Letter |

    Translation termination sequences are occasionally bypassed by the ribosome and the resulting proteins can be detrimental to the cell; here it is shown that cells can prevent such proteins from accumulating through peptides that are encoded within the 3' UTR of genes in both humans and C. elegans.

    • Joshua A. Arribere
    • , Elif S. Cenik
    •  & Andrew Z. Fire

  • Article |

    The genes encoding the subunits of oxidative phosphorylation complexes are split between the nuclear and mitochondrial genomes, but their translation is synchronized by signalling from the cytosol to the mitochondria.

    • Mary T. Couvillion
    • , Iliana C. Soto
    •  & L. Stirling Churchman

  • Letter |

    The structure of a bacterial ribosome–RelA complex reveals that RelA, a protein recruited to the ribosome in the case of scarce amino acids, binds in a different location to translation factors, and that this binding event suppresses auto-inhibition to activate synthesis of the (p)ppGpp secondary messenger, thus initiating stringent control.

    • Alan Brown
    • , Israel S. Fernández
    •  & V. Ramakrishnan

  • Article |

    Defects in the ribosome quality control (RQC) complex, which clears proteins that stalled during translation, can cause neurodegeneration; here it is shown that in RQC-defective cells a peptide tail added by the RQC subunit 2 to stalled polypeptides promotes their aggregation and the sequestration of chaperones in these aggregates, affecting normal protein quality control processes.

    • Young-Jun Choe
    • , Sae-Hun Park
    •  & F. Ulrich Hartl

  • Letter |

    The crystal structure of Schizosaccharomyces pombe guanine nucleotide exchange factor eIF2B, providing a structural framework for the eIF2B-mediated mechanism of stress-induced translational control.

    • Kazuhiro Kashiwagi
    • , Mari Takahashi
    •  & Shigeyuki Yokoyama

  • Letter |

    Tumours can require certain amino acids for their proliferation, and the diricore method described here helps to identify such restrictive amino acids; using this method in kidney cancer tissue and breast carcinoma cells, the authors observe an association between proline deficiency and upregulation of PYCR1, an enzyme required for proline synthesis.

    • Fabricio Loayza-Puch
    • , Koos Rooijers
    •  & Reuven Agami

  • Article |

    In-depth analyses of protein expression studies are used to derive a new codon-influence metric that correlates with global protein levels, mRNA levels and mRNA lifetimes in vivo, indicating tight coupling between translation efficiency and mRNA stability; genes redesigned based on these analyses consistently yield high protein expression levels both in vivo and in vitro.

    • Grégory Boël
    • , Reka Letso
    •  & John F. Hunt

  • Letter |

    Under stress, such as heat shock, the N6-methyladenosine (m6A) modification is shown to accumulate primarily in the 5′ untranslated region of induced mRNAs owing to the translocation of an m6A interacting protein, YTHDF2, into the nucleus, resulting in increased cap-independent translation of these mRNAs, indicating one possible mechanism by which stress-responsive genes can be preferentially expressed.

    • Jun Zhou
    • , Ji Wan
    •  & Shu-Bing Qian

  • Article |

    The cryo-electron microscopy structure of the eukaryotic initiation factor 3 (eIF3) within the larger 43S complex is determined; the improved resolution enables visualization of the secondary structures of the subunits, as well as the contacts between eIF3 and both eIF2 and DHX29.

    • Amedee des Georges
    • , Vidya Dhote
    •  & Yaser Hashem

  • Letter |

    All eukaryotes utilize a single termination factor, eRF1, to halt translation when the ribosome encounters one of three possible stop codons; here electron cryo-microscopy structures of ribosome–eRF1 complexes in the process of recognizing each stop codon reveal how stop codons are discriminated from sense codons.

    • Alan Brown
    • , Sichen Shao
    •  & V. Ramakrishnan

  • Letter |

    A ribosome with tethered subunits, ‘Ribo-T’, is engineered by making a hybrid RNA composed of ribosomal RNA of large and small subunits; Ribo-T can support cell growth in vivo in the absence of wild-type ribosomes, and is used to establish a fully orthogonal ribosome–mRNA system.

    • Cédric Orelle
    • , Erik D. Carlson
    •  & Alexander S. Mankin

  • Article |

    The structure of the human ribosome at high resolution has been solved; by combining single-particle cryo-EM and atomic model building, local resolution of 2.9 Å was achieved within the most stable areas of the structure.

    • Heena Khatter
    • , Alexander G. Myasnikov
    •  & Bruno P. Klaholz

  • Letter |

    Eukaryotic initiation factor 3 (eIF3)—the deregulation of which has been linked with diverse cancers—is shown to bind to and direct the specialized translation of a subset of messenger RNAs, primarily involved in cell proliferation, differentiation and apoptosis, and can exert either translational activation or repression.

    • Amy S. Y. Lee
    • , Philip J. Kranzusch
    •  & Jamie H. D. Cate

  • Letter |

    A single particle cryo-EM structure of the 70S ribosome in complex with the elongation factor Tu breaks the 3 Å resolution barrier of the technique and locally exceeds the resolution of previous crystallographic studies, revealing all modifications in rRNA and explaining their roles in ribosome function and antibiotic binding.

    • Niels Fischer
    • , Piotr Neumann
    •  & Holger Stark

  • Letter |

    A new mechanism that plants use to combat begomoviruses—one of the most pathogenic groups of plant viruses, causing severe disease in major crops worldwide—is uncovered: plants inhibit the transcription of genes associated with the translational apparatus, thus causing a general reduction in protein synthesis.

    • Cristiane Zorzatto
    • , João Paulo B. Machado
    •  & Elizabeth P. B. Fontes

  • Letter |

    A eukaryotic viral internal ribosome entry site (IRES) element is described that binds both bacterial and eukaryotic ribosomes and initiates translation in both, demonstrating that RNA structure-based initiation can occur in both these domains of life, although in bacteria the element uses a mechanism that differs from that in eukaryotes.

    • Timothy M. Colussi
    • , David A. Costantino
    •  & Jeffrey S. Kieft

  • Article |

    Specialized ribosomes (with a particular protein composition) carry out translation of specific transcripts; analysis of Hox mRNA translation in mice reveals that unique RNA structural elements within their 5′ UTRs, including internal ribosome entry sites and translation inhibitory elements, are responsible for this specialized mode of translation.

    • Shifeng Xue
    • , Siqi Tian
    •  & Maria Barna

  • Letter |

    The mTORC1 complex has been implicated in tumorigenesis owing partially to its ability to increase protein translation; now, mTORC1 activity in the mouse intestine is shown not to be required for normal homeostasis but to be necessary for the triggering of tumorigenesis by APC mutations, suggesting that it could be a good target for the prevention of colorectal cancer in high-risk patients.

    • William J. Faller
    • , Thomas J. Jackson
    •  & Owen J. Sansom

  • Letter |

    The structure of the 39S large mitoribosome subunit is solved by cryo-electron microscopy at an impressive 3.4 Å resolution, revealing the location of 50 ribosomal proteins, the peptidyl transferase centre, the tRNAs within this active site, and the nascent peptide chain within the exit tunnel.

    • Basil J. Greber
    • , Daniel Boehringer
    •  & Nenad Ban

  • Article |

    Whereas previous structural investigation of ribosome inhibitors has been done using the prokaryotic ribosome, this work presents X-ray crystal structures of the yeast ribosome in complex with 16 inhibitors including eukaryotic-specific inhibitors; the inhibitors all bind the mRNA or tRNA binding sites, larger molecules appear to target specifically the first elongation cycle.

    • Nicolas Garreau de Loubresse
    • , Irina Prokhorova
    •  & Marat Yusupov

  • Letter |

    The crystal structure of the RNA binding domains of Sxl and Unr with msl2 RNA shows that interwoven interactions establish cooperative assembly of the ternary complex, highlighting how binding of relatively general RNA binding domains to RNA can result in a unique and specific protein–RNA architecture.

    • Janosch Hennig
    • , Cristina Militti
    •  & Michael Sattler

  • Letter |

    Transcription and translation are generally thought of as disconnected processes in eukaryotes; however, under starvation conditions in yeast, the promoter sequence influences not only messenger RNA levels but also several processes downstream of transcription, including the localization of mRNA within the cytoplasm and the translation rate of mRNA.

    • Brian M. Zid
    •  & Erin K. O’Shea

  • Letter |

    To investigate the mechanism of frameshifting during messenger RNA translation, a technique was developed to monitor translation of single molecules in real time using Förster resonance energy transfer (FRET); ribosomes were revealed to pause tenfold longer than usual during elongation at the frameshifting sites.

    • Jin Chen
    • , Alexey Petrov
    •  & Joseph D. Puglisi

  • Article |

    A new high-throughput sequencing method to determine mRNA poly(A)-tail length enabled studies of individual RNAs across species and developmental stages to investigate the role of poly(A) length in translational regulation; the relationship between poly(A) length and translational efficiency shown in early embryo systems does not occur later in development, a finding that explains different regulatory consequences of microRNAs acting at different developmental times.

    • Alexander O. Subtelny
    • , Stephen W. Eichhorn
    •  & David P. Bartel

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