PPR proteins shed a new light on RNase P biology.
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.
Institut de Biologie Moléculaire des Plantes du CNRS; Université de Strasbourg; Strasbourg, France; Institut de Biologie Moléculaire et Cellulaire du CNRS; Architecture et Réactivité de l'ARN; Université de Strasbourg; Strasbourg, France.
Franziska
F
Pinker
Institut de Biologie Moléculaire des Plantes du CNRS; Université de Strasbourg; Strasbourg, France.
Géraldine
G
Bonnard
Institut de Biologie Moléculaire des Plantes du CNRS; Université de Strasbourg; Strasbourg, France.
Anthony
A
Gobert
Institut de Biologie Moléculaire des Plantes du CNRS; Université de Strasbourg; Strasbourg, France.
Bernard
B
Gutmann
Institut de Biologie Moléculaire des Plantes du CNRS; Université de Strasbourg; Strasbourg, France.
Kamel
K
Hammani
Institut de Biologie Moléculaire et Cellulaire du CNRS; Architecture et Réactivité de l'ARN; Université de Strasbourg; Strasbourg, France.
Claude
C
Sauter
Department of Molecular Biosciences; University of Kansas;Lawrence, KS USA.
Peter A
PA
Gegenheimer
Institut de Biologie Moléculaire des Plantes du CNRS; Université de Strasbourg; Strasbourg, France.
Philippe
P
Giegé
D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism; D002467:Cell Nucleus / Q000235:genetics / Q000378:metabolism; D002736:Chloroplasts / Q000235:genetics / Q000378:metabolism; D005057:Eukaryotic Cells / Q000378:metabolism; D006801:Humans; D008928:Mitochondria / Q000235:genetics / Q000378:metabolism; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012322:RNA Precursors / Q000235:genetics / Q000378:metabolism; D012343:RNA, Transfer / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D043262:Ribonuclease P / Q000235:genetics / Q000378:metabolism*; D014346:Trypanosoma brucei brucei / Q000235:genetics / Q000378:metabolism
D029681:Arabidopsis Proteins; D010940:Plant Proteins; D012322:RNA Precursors; D016601:RNA-Binding Proteins; D012343:RNA, Transfer; C581753:PRORP1 protein, Arabidopsis; D043262:Ribonuclease P
RNA binding protein; RNase P; evolution; pentatricopeptide repeat; tRNA maturation