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Showing 1–9 of 9 results
Advanced filters: Author: Philippe Giegé Clear advanced filters

  • New approaches to plant disease control are important for pathogens that are difficult to control by existing methods. Here, the authors report a potential strategy to combat plant viruses by cytosolic expressed protein-only RNase P and show its ability for in vitro cleavage of tRNA-like structures existing in many plant viruses.

    • Anthony Gobert
    • Yifat Quan
    • Philippe Giegé
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-6

  • Mitoribosomes are remarkably diverse in their structures and compositions. Here the authors combine biochemistry, genetics, single particle cryo-electron microscopy and in situ cryo-electron tomography to reveal the mitochondrial ribosome of Chlamydomonas reinhardtii as an extreme example of evolution and species-specific adaptation.

    • Florent Waltz
    • Thalia Salinas-Giegé
    • Yaser Hashem
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-15

  • This study shows that the tRNA-modifying enzymes TRM1A/TRM1B are essential to attain the steady-state pool of tRNAs and reveals how they functionally cooperate with RNase P in vivo for the early steps of tRNA biogenesis in Arabidopsis.

    • Mathilde Arrivé
    • Mathieu Bruggeman
    • Philippe Giegé
    Research
    Nature Plants
    Volume: 9, P: 2031-2041

  • RNase Ps are involved in tRNA maturation and are typically found to be ribonucleoproteins. An essential Arabidopsis thaliana organellar protein is now found to possess RNase P activity and be able to replace the E. coli ribonucleoprotein RNase P.

    • Anthony Gobert
    • Bernard Gutmann
    • Philippe Giegé
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 740-744

  • This study characterized the unique protein subunit composition and structure of Arabidopsis mitochondrial ribosomes using biochemical assays and cryo-electron microscopy. Ten subunits are pentatricopeptide (PPR) proteins, among which rPPR1 functions as a translation factor.

    • Florent Waltz
    • Tan-Trung Nguyen
    • Philippe Giegé
    Research
    Nature Plants
    Volume: 5, P: 106-117

  • RNase P is a key enzyme implicated in transfer RNA maturation that removes the 5′-leader sequences from transfer RNA precursors. In this study, a biophysical characterization of a novel protein-only variant of RNase P, known as PRORP (PROteinaceous RNase P), reveals that transfer RNA recognition by PRORP is similar to that by ribonucleoprotein RNase P.

    • Anthony Gobert
    • Franziska Pinker
    • Philippe Giegé
    ResearchOpen Access
    Nature Communications
    Volume: 4, P: 1-8

  • Mitochondria ribosomes translate essential mRNAs encoded by mitochondrial genomes. The cryo-EM structure of the 78S mitoribosome from cauliflower shows plant-specific pentatricopeptide repeat proteins binding rRNAs expanded over those of animals.

    • Florent Waltz
    • Heddy Soufari
    • Yaser Hashem
    Research
    Nature Plants
    Volume: 6, P: 377-383