PRORP proteins support RNase P activity in both organelles and the nucleus in Arabidopsis

• DOI: 10.1101/gad.189514.112
• Publication Date: 2012-05-02T02:43:37Z
• Authors: Bernard Gutmann; Anthony Gobert; Philippe Giegé
• Keywords: Cell Nucleus; Arabidopsis Proteins; Arabidopsis; [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology; [SDV.BC]Life Sciences [q-bio]/Cellular Biology; [SDV.BBM.BM] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology; Ribonuclease P; Mitochondria; RNA, Transfer; Ribonucleoproteins; [SDV.BV]Life Sciences [q-bio]/Vegetal Biology; RNA, Small Nucleolar; [SDV.BV] Life Sciences [q-bio]/Vegetal Biology; RNA, Messenger; RNA Processing, Post-Transcriptional; tRNA; [SDV.BC] Life Sciences [q-bio]/Cellular Biology

RNase P is an essential enzyme that cleaves the 5′ leader sequence of tRNA precursors. RNase Ps were believed until now to occur universally as ribonucleoproteins in organisms performing RNase P activity. Here we find that protein-only RNase P enzymes called PRORP (for proteinaceous RNase P) support RNase P activity in vivo in both organelles and the nucleus in Arabidopsis. Beyond tRNA, PRORP proteins are involved in the maturation of small nucleolar RNA (snoRNA) and mRNA. Finally, ribonucleoprotein RNase MRP is not involved in tRNA maturation in plants. Altogether, our results indicate that ribonucleoprotein enzymes have been entirely replaced by proteins for RNase P activity in plants.