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Showing 1–9 of 9 results
Advanced filters: Author: Naohiro Terasaka Clear advanced filters

  • The authors develop a ribozyme, Tx2.1, that is capable of aminoacylating tRNA with specificity for the anticodon from directed evolution of a T-box riboswitch. Tx2.1 could be used to charge non-natural amino acids in an in vitro translation system.

    • Satoshi Ishida
    • Naohiro Terasaka
    • Hiroaki Suga
    Research
    Nature Chemical Biology
    Volume: 16, P: 702-709

  • Archaea use a tRNAIle with agmatine conjugated at the C34 position to decode the AUA codon. The enzyme that catalyzes this reaction, TiaS, has been previously identified, and it is now shown that it uses a novel kinase domain to hydrolyze ATP into AMP and pyrophosphate before phosphorylating itself and the tRNA on its way to conjugating the agmatine.

    • Naohiro Terasaka
    • Satoshi Kimura
    • Tsutomu Suzuki
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 1268-1274

  • Detailed analysis of multiscale structures and the identification of long-lived streamer-like wavemodes in a magnetically confined plasma provides new insight into the physics of plasma turbulence.

    • Takuma Yamada
    • Sanae-I. Itoh
    • Kimitaka Itoh
    Research
    Nature Physics
    Volume: 4, P: 721-725

  • In vitro screening of a ribosomally synthesized macrocyclic peptide library containing cyclic γ2,4-amino acids (cγAA) afforded the discovery of potent inhibitors of the SARS-CoV-2 main protease (Mpro). A co-crystal structure revealed the contribution of this cγAA to Mpro binding and the proteolytic stability of these macrocycles.

    • Takashi Miura
    • Tika R. Malla
    • Hiroaki Suga
    ResearchOpen Access
    Nature Chemistry
    Volume: 15, P: 998-1005

  • Established bacterial glycoengineering platforms limit access to protein and glycan substrates. Here the authors design a cytoplasmic protein glycosylation system, Glycoli, to generate a variety of multivalent glycostructures.

    • Hanne L. P. Tytgat
    • Chia-wei Lin
    • Timothy G. Keys
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-10

  • Genetic code reprogramming has generally focused on changing the translation step of protein expression, altering what each codon specifies. Mutations in the peptidyl transferase center, along with compensatory mutations in the C-termini of tRNAs, now provide an alternate method to create fully orthogonal ribosomes.

    • Naohiro Terasaka
    • Gosuke Hayashi
    • Hiroaki Suga
    Research
    Nature Chemical Biology
    Volume: 10, P: 555-557

  • TiaS catalyzes the transfer of agmatine onto the first position cytidine of the tRNAIle2 anticodon in archaea, ensuring proper translation of the matching codon. Now the crystal structures of the TiaS–tRNAIle2 complex with ATP, or with AMPCPP and agmatine, reveal a novel kinase domain and show how TiaS selects the correct tRNA while segregating the target cytidine until agmatine is bound.

    • Takuo Osawa
    • Satoshi Kimura
    • Tomoyuki Numata
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 1275-1280