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Showing 1–13 of 13 results
Advanced filters: Author: Takuhiro Ito Clear advanced filters

  • 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
    Research
    Nature
    Volume: 467, P: 612-616

  • The marine natural product girolline is an inhibitor of protein synthesis. Here, the authors show that girolline is a sequence-selective modulator of eIF5A that can cause ribosome stalling and activate ribosome-associated quality control.

    • Tilman Schneider-Poetsch
    • Yongjun Dang
    • Minoru Yoshida
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-13

  • The plant AUG-stop element in the 5′ UTR acts as a boron concentration sensor, regulating downstream ORF translation. Here, structural and biochemical analyses show that a high concentration of borate fixes eRF1 on 80S ribosomes, preventing sliding through downstream of AUG-stop elements.

    • Mayuki Tanaka
    • Takeshi Yokoyama
    • Toru Fujiwara
    Research
    Nature Chemical Biology
    Volume: 20, P: 605-614

  • Here the authors show that a viral protein interferes with the binding of phosphorylated eIF2 to eIF2B, thereby suppressing the host integrated stress response (ISR). This suppression of the ISR abrogates translational changes of the host and ameliorates neurite degradation under stress.

    • Kazuhiro Kashiwagi
    • Yuichi Shichino
    • Takuhiro Ito
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-12

  • The integrated stress response affects cell survival or death under stress conditions, and depends on the activity of the eukaryotic translation initiation factor eIF2B. New research identifies a protein helix that modulates this response by controlling the structural states of eIF2B.

    • Kazuhiro Kashiwagi
    • Takuhiro Ito
    News & Views
    Nature Chemical Biology
    Volume: 20, P: 394-395

  • The maturation of tRNAs involves folding into their L shape and nucleotide modifications at several positions. Some modifying enzymes require an L-shaped substrate, and the crystal structure of methylase Trm5 in complex with AdoMet and tRNA now reveals how the substrate tertiary structure is sensed.

    • Sakurako Goto-Ito
    • Takuhiro Ito
    • Shigeyuki Yokoyama
    Research
    Nature Structural & Molecular Biology
    Volume: 16, P: 1109-1115

  • 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
    Research
    Nature
    Volume: 531, P: 122-125

  • Alternative pre-mRNA splicing is often jointly controlled by multiple splicing factors. Here Muto and colleagues elucidate the structural basis for cooperative RNA recognition by two splicing regulators required for tissue-specific expression of C. elegans FGFR.

    • Kanako Kuwasako
    • Mari Takahashi
    • Yutaka Muto
    Research
    Nature Structural & Molecular Biology
    Volume: 21, P: 778-786

  • The structurally constrained knotted configuration of the RNA methyltransferase TrmD captures the free energy of substrate binding to facilitate catalysis.

    • Thomas Christian
    • Reiko Sakaguchi
    • Ya-Ming Hou
    Research
    Nature Structural & Molecular Biology
    Volume: 23, P: 941-948