Structural insights into protein-only RNase P complexed with tRNA

Anthony Gobert, Franziska Pinker, Olivier Fuchsbauer, Bernard Gutmann, René Boutin, Pierre Roblin, Claude Sauter () and Philippe Giegé ()
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Anthony Gobert: Institut de Biologie Moléculaire des Plantes du CNRS, Université de Strasbourg, 12 rue du Général Zimmer, 67084 Strasbourg, France
Franziska Pinker: Institut de Biologie Moléculaire des Plantes du CNRS, Université de Strasbourg, 12 rue du Général Zimmer, 67084 Strasbourg, France
Olivier Fuchsbauer: Institut de Biologie Moléculaire et Cellulaire du CNRS, Architecture et Réactivité de l'ARN, Université de Strasbourg
Bernard Gutmann: Institut de Biologie Moléculaire des Plantes du CNRS, Université de Strasbourg, 12 rue du Général Zimmer, 67084 Strasbourg, France
René Boutin: Laboratoire d’Hydrologie et de Géochimie du CNRS
Pierre Roblin: Synchrotron SOLEIL, l'Orme des Merisiers Saint-Aubin
Claude Sauter: Institut de Biologie Moléculaire et Cellulaire du CNRS, Architecture et Réactivité de l'ARN, Université de Strasbourg
Philippe Giegé: Institut de Biologie Moléculaire des Plantes du CNRS, Université de Strasbourg, 12 rue du Général Zimmer, 67084 Strasbourg, France

Nature Communications, 2013, vol. 4, issue 1, 1-8

Abstract: Abstract RNase P is the essential activity removing 5′-leader sequences from transfer RNA precursors. RNase P was always associated with ribonucleoprotein complexes before the discovery of protein-only RNase P enzymes called PRORPs (PROteinaceous RNase P) in eukaryotes. Here we provide biophysical and functional data to understand the mode of action of PRORP enzymes. Activity assays and footprinting experiments show that the anticodon domain of transfer RNA is dispensable, whereas individual residues in D and TψC loops are essential for PRORP function. PRORP proteins are characterized in solution and a molecular envelope is derived from small-angle X-ray scattering. Conserved residues are shown to be involved in the binding of one zinc atom to PRORP. These results facilitate the elaboration of a model of the PRORP/transfer RNA interaction. The comparison with the ribonucleoprotein RNase P/transfer RNA complex suggests that transfer RNA recognition by PRORP proteins is similar to that by ribonucleoprotein RNase P.

Date: 2013
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms2358

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DOI: 10.1038/ncomms2358

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