tRNAs articles within Nature

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  • Article
    | Open Access

    tRNA display enables the direct selection of orthogonal aminoacyl-tRNA synthetases that acylate orthogonal tRNAs with non-canonical monomers, enabling in vivo synthesis of proteins that include these monomers and expanding the repertoire of the genetic code.

    • Daniel L. Dunkelmann
    • , Carlos Piedrafita
    •  & Jason W. Chin

  • Article
    | Open Access

    Suppressor tRNAs adapted to the amino acid that they carry enable readthrough of premature termination codons introduced by nonsense mutations and show potential for the treatment of genetic diseases such as cystic fibrosis.

    • Suki Albers
    • , Elizabeth C. Allen
    •  & Zoya Ignatova

  • Article |

    Analyses of in-frame stop codons in protein-coding genes of Blastocrithidia nonstop with all three stop codons reassigned reveal a mechanism for UGA reassignment in eukaryotes involving shortening of the tRNA anticodon stem and a mutant eRF1 release factor.

    • Ambar Kachale
    • , Zuzana Pavlíková
    •  & Julius Lukeš

  • Article |

    Structures of the human METTL1–WDR4 complex are revealed, providing molecular insights into substrate recognition, modification and catalytic regulation by the N7-methylguanosine methyltransferase complex.

    • Jiazhi Li
    • , Longfei Wang
    •  & Richard I. Gregory

  • 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

  • Letter |

    Members of the SAM-dependent methyltransferase superfamily are involved in the modification of wobble uridine to 5-oxacetyl uridine in Gram-negative bacteria; CmoA converts SAM to carboxy-SAM (Cx-SAM; a metabolite that was unknown previously), and CmoB uses Cx-SAM to convert 5-hydroxyuridine to 5-oxyacetyl uridine in tRNA.

    • Jungwook Kim
    • , Hui Xiao
    •  & Steven C. Almo

  • Letter |

    The frq gene, essential for circadian clock function, is shown to differ from most other genes in Neurospora by exhibiting non-optimal codon usage; by contrast, optimization of codon usage is unexpectedly found to affect the structure and function of the coded protein, subsequently impairing circadian feedback loops.

    • Mian Zhou
    • , Jinhu Guo
    •  & Yi Liu

  • Letter |

    An integrated mechanism for decoding is proposed, based on six X-ray structures of the 70S ribosome determined at 3.1–3.4 Å resolution, modelling cognate or near-cognate states of the decoding centre at the proofreading step.

    • Natalia Demeshkina
    • , Lasse Jenner
    •  & Gulnara Yusupova

  • Letter |

    During translation, tRNAs enter the ribosome and then move sequentially through three sites, known as A, P and E, as they transfer their attached amino acids onto the growing peptide chain. How the ribosome facilitates tRNA translocation between the sites remains largely unknown. Now a study uses multiparticle cryoelectron microscopy of a ribosome bound to the translation elongation factor, EF-G, to get information about tRNA movement. It identifies two new substates and sees that translocation is linked to unratcheting of the 30S ribosomal subunit.

    • Andreas H. Ratje
    • , Justus Loerke
    •  & Christian M. T. Spahn

  • Article |

    tRNAs are synthesized in a premature form that requires trimming of the 5′ and 3′ ends and modification of specific nucleotides. RNase P, a complex containing a long catalytic RNA and a protein cofactor, catalyses the cleavage that generates the mature 5′ end. Here, the structure of RNase P bound to mature tRNAPhe is solved. Recognition of the leader sequence and its mechanism of cleavage is determined by soaking an oligonucleotide corresponding to the premature 5′ end into the crystal.

    • Nicholas J. Reiter
    • , Amy Osterman
    •  & Alfonso Mondragón

  • Letter |

    In most bacteria and all archaea, glutamyl-tRNA synthetase (GluRS) glutamylates both tRNAGlu and tRNAGln; Glu-tRNAGln is then converted to Gln-tRNAGln by an amidotransferase. Here the structure is reported of a bacterial complex containing tRNAGln, GluRS and the amidotransferase GatCAB. The structure provides an explanation for how the enzymes work consecutively: only one can assume a productive state at any time. There also seems to be an intermediary state in which neither enzyme is productive.

    • Takuhiro Ito
    •  & Shigeyuki Yokoyama

  • Letter |

    Tail-anchored proteins have a single transmembrane domain at their carboxy termini and are post-translationally targeted to the endoplasmic reticulum via the cytosolic ATPase TRC40. These authors identify a conserved protein complex called Bat3 complex that is recruited to ribosomes, interacts with the transmembrane domain of newly released tail-anchored proteins and transfers them to TRC40 for subsequent targeting to the endoplasmic reticulum.

    • Malaiyalam Mariappan
    • , Xingzhe Li
    •  & Ramanujan S. Hegde

  • Article |

    Single-molecule studies allow biological processes to be examined one molecule at a time, as they occur. Here, zero-mode waveguides have been used to concentrate reactions in zeptolitre-sized volumes, making it possible to study real-time translocation by the ribosome. The binding of transfer RNAs (tRNAs) to the ribosome could be followed; the results show that tRNA release from the exit site is uncoupled from tRNA binding to the aminoacyl-tRNA site.

    • Sotaro Uemura
    • , Colin Echeverría Aitken
    •  & Joseph D. Puglisi

  • Letter |

    Evolution from one fitness peak to another must involve either transitions through intermediates of low fitness or skirting round the fitness valley through compensatory mutations elsewhere. Here, the base pairs in mitochondrial tRNA stems is used as a model to show that deep fitness valleys can be traversed. Transitions between AU and GC pairs have occurred during mammalian evolution without help from genetic drift or mutations elsewhere.

    • Margarita V. Meer
    • , Alexey S. Kondrashov
    •  & Fyodor A. Kondrashov

  • Letter |

    Although new amino acids with desirable properties can be devised, only a few have been successfully introduced into proteins by the cellular machinery. Even then, only one type of unnatural amino acid can be added to a given protein. Here, a new system has been designed that could allow the incorporation of up to 200 novel amino acids. The system involves an orthogonal ribosome that uses quadruplet — rather than triplet — codons, as well as orthogonal tRNA synthetase–tRNA pairs.

    • Heinz Neumann
    • , Kaihang Wang
    •  & Jason W. Chin

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