PPR proteins shed a new light on RNase P biology
| Autor: | Géraldine Bonnard, Franziska Pinker, Bernard Gutmann, Philippe Giegé, Peter Gegenheimer, Claude Sauter, Kamel Hammani, Anthony Gobert |
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| Rok vydání: | 2013 |
| Předmět: |
Chloroplasts
Protein Conformation RNase P Trypanosoma brucei brucei RNA-binding protein Review Biology RNase PH Ribonuclease P tRNA maturation RNA Transfer evolution RNA Precursors Humans Molecular Biology Plant Proteins Ribonucleoprotein Cell Nucleus Genetics Arabidopsis Proteins RNA-Binding Proteins RNA Cell Biology RNA binding protein Mitochondria Protein Structure Tertiary RNase MRP Eukaryotic Cells pentatricopeptide repeat Biochemistry Transfer RNA Pentatricopeptide repeat |
| Zdroj: | RNA Biology |
| ISSN: | 1555-8584 1547-6286 |
| DOI: | 10.4161/rna.25273 |
| Popis: | A fast growing number of studies identify pentatricopeptide repeat (PPR) proteins as major players in gene expression processes. Among them, a subset of PPR proteins called PRORP possesses RNase P activity in several eukaryotes, both in nuclei and organelles. RNase P is the endonucleolytic activity that removes 5′ leader sequences from tRNA precursors and is thus essential for translation. Before the characterization of PRORP, RNase P enzymes were thought to occur universally as ribonucleoproteins, although some evidence implied that some eukaryotes or cellular compartments did not use RNA for RNase P activity. The characterization of PRORP reveals a two-domain enzyme, with an N-terminal domain containing multiple PPR motifs and assumed to achieve target specificity and a C-terminal domain holding catalytic activity. The nature of PRORP interactions with tRNAs suggests that ribonucleoprotein and protein-only RNase P enzymes share a similar substrate binding process. |
| Databáze: | OpenAIRE |
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