Determination of protein-only RNase P interactome in Arabidopsis mitochondria and chloroplasts identifies a complex between PRORP1 and another NYN domain nuclease.
Fiche publication
Date publication
juillet 2019
Journal
The Plant journal : for cell and molecular biology
Auteurs
Membres identifiés du Cancéropôle Est :
Mr HAMMANN Philippe
Tous les auteurs :
Bouchoucha A, Waltz F, Bonnard G, Arrivé M, Hammann P, Kuhn L, Schelcher C, Zuber H, Gobert A, Giegé P
Lien Pubmed
Résumé
The essential endonuclease activity that removes 5' leader sequences from transfer RNA precursors is called RNase P. While ribonucleoprotein RNase P enzymes containing a ribozyme are found in all domains of life, another type of RNase P called "PRORP", for "PROtein-only RNase P", only composed of protein occurs in a wide variety of eukaryotes, in organelles and the nucleus. Here, in order to find how PRORP functions integrate with other cell processes, we exemplarily explore the protein interaction network of PRORP1 in Arabidopsis mitochondria and chloroplasts. Although PRORP proteins function as single subunit enzymes in vitro, we find that PRORP1 occurs in protein complexes and is present in high molecular weight fractions containing mitochondrial ribosomes. The analysis of immuno-precipitated protein complexes identifies proteins involved in organellar gene expression processes. In particular, direct interaction is established between PRORP1 and MNU2 a mitochondrial nuclease. A specific domain of MNU2 and a conserved signature of PRORP1 are found to be directly accountable for this protein interaction. Altogether, results reveal the existence of an RNA maturation complex in Arabidopsis mitochondria and suggest that PRORP proteins cooperate with other gene expression factors for RNA maturation in vivo. This article is protected by copyright. All rights reserved.
Mots clés
RNA maturation, RNase P, mitochondrial nucleases, pentatricopeptide repeats
Référence
Plant J.. 2019 Jul 18;: