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RNA Biol. 2013;10(9):1457-68. doi: 10.4161/rna.25273. Epub 2013 Jun 19.

PPR proteins shed a new light on RNase P biology.

Author information

1
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.
2
Institut de Biologie Moléculaire des Plantes du CNRS; Université de Strasbourg; Strasbourg, France.
3
Institut de Biologie Moléculaire et Cellulaire du CNRS; Architecture et Réactivité de l'ARN; Université de Strasbourg; Strasbourg, France.
4
Department of Molecular Biosciences; University of Kansas;Lawrence, KS USA.

Abstract

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.

KEYWORDS:

RNA binding protein; RNase P; evolution; pentatricopeptide repeat; tRNA maturation

PMID:
23925311
PMCID:
PMC3858429
DOI:
10.4161/rna.25273
[Indexed for MEDLINE]
Free PMC Article

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