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Showing 1–12 of 12 results
Advanced filters: Author: Lasse Jenner Clear advanced filters

  • A series of eight crystal structures shows the changes that occur in interactions between the bacterial 70S ribosome and the messenger RNA during translation initiation, post-initiation and elongation. Certain interactions are only observed when the Shine–Dalgarno sequence is present, and the exit path of the mRNA appears to change once translation shifts from initiation to elongation mode.

    • Gulnara Yusupova
    • Lasse Jenner
    • Marat Yusupov
    Research
    Nature
    Volume: 444, P: 391-394

  • Ensuring the ribosome accepts a correct tRNA is key to fidelity of translation. The structures of the 70S ribosome carrying correct and incorrect tRNAs are now presented, giving mechanistic insight into the tRNA proofreading process where ribosomal proteins are shown to play an active role.

    • Lasse Jenner
    • Natalia Demeshkina
    • Marat Yusupov
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 1072-1078

  • 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
    Research
    Nature
    Volume: 484, P: 256-259

  • The accuracy of eukaryotic ribosome translocation relies on eukaryote-specific elements of the 80S ribosome, elongation factor 2 and transfer RNAs, all of which contribute to the maintenance of the messenger RNA reading frame.

    • Nemanja Milicevic
    • Lasse Jenner
    • Gulnara Yusupova
    Research
    Nature
    Volume: 625, P: 393-400

  • Structural analysis of the Saccharomyces cerevisiae 80S ribosome trapped in an intermediate translocation state shows stabilization of codon–anticodon interactions by eukaryote-specific elements of the 80S ribosome, eEF2 and tRNA and demonstrates a major role for eEF2 in maintaining the directionality of translocation.

    • Muminjon Djumagulov
    • Natalia Demeshkina
    • Gulnara Yusupova
    ResearchOpen Access
    Nature
    Volume: 600, P: 543-546

  • Complement 5 (C5) generates the C5a anaphylatoxin and C5b, a component of the membrane attack complex. Andersen and colleagues present the crystal structure of C5 and identify similarities and differences between C5 and other complement proteins.

    • Folmer Fredslund
    • Nick S Laursen
    • Gregers R Andersen
    Research
    Nature Immunology
    Volume: 9, P: 753-760

  • During stress conditions bacterial ribosomes dimerize and form inactive but stable hibernating 100S particles, a process that is facilitated by the hibernation-promoting factor (HPF). Here the authors analyze 100S dimer formation as a function of HPF protein concentration and present the Thermus thermophilus 100S ribosome cryo-EM structure.

    • Rasmus Kock Flygaard
    • Niels Boegholm
    • Lasse B. Jenner
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-12

  • An important aspect of translational fidelity is that the reading frame of a translating mRNA be maintained on the ribosome. Structures representing the initiating and elongating ribosome now show that a tunnel narrows to facilitate a network of interactions that may hold the message in frame in the latter complex.

    • Lasse B Jenner
    • Natalia Demeshkina
    • Marat Yusupov
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 555-560

  • 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.

    • Sergey Melnikov
    • Adam Ben-Shem
    • Marat Yusupov
    Reviews
    Nature Structural & Molecular Biology
    Volume: 19, P: 560-567