PPR proteins shed a new light on RNase P biology.

作者: Franziska Pinker , Géraldine Bonnard , Anthony Gobert , Bernard Gutmann , Kamel Hammani

DOI: 10.4161/RNA.25273

关键词: BiologyRNA-binding proteinRNase MRPRNase PBiochemistryTransfer RNARNAGeneticsPentatricopeptide repeatRibonucleoproteinRNase PH

摘要: A fast growing number of studies identify pentatricopeptide repeat (PPR) proteins as major players in gene expression processes. Among them, a subset PPR called PRORP possesses RNase P activity several eukaryotes, both nuclei and organelles. is the endonucleolytic that removes 5′ leader sequences from tRNA precursors thus essential for translation. Before characterization PRORP, enzymes were thought to occur universally ribonucleoproteins, although some evidence implied eukaryotes or cellular compartments did not use RNA activity. The reveals two-domain enzyme, with an N-terminal domain containing multiple motifs assumed achieve target specificity C-terminal holding catalytic nature interactions tRNAs suggests ribonucleoprotein protein-only share similar substrate binding process.

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