Cargando…
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...
Autores principales: | , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Landes Bioscience
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3858429/ https://www.ncbi.nlm.nih.gov/pubmed/23925311 http://dx.doi.org/10.4161/rna.25273 |
_version_ | 1782295284625178624 |
---|---|
author | Pinker, Franziska Bonnard, Géraldine Gobert, Anthony Gutmann, Bernard Hammani, Kamel Sauter, Claude Gegenheimer, Peter A Giegé, Philippe |
author_facet | Pinker, Franziska Bonnard, Géraldine Gobert, Anthony Gutmann, Bernard Hammani, Kamel Sauter, Claude Gegenheimer, Peter A Giegé, Philippe |
author_sort | Pinker, Franziska |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-3858429 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Landes Bioscience |
record_format | MEDLINE/PubMed |
spelling | pubmed-38584292013-12-16 PPR proteins shed a new light on RNase P biology Pinker, Franziska Bonnard, Géraldine Gobert, Anthony Gutmann, Bernard Hammani, Kamel Sauter, Claude Gegenheimer, Peter A Giegé, Philippe RNA Biol Review 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. Landes Bioscience 2013-09-01 2013-06-19 /pmc/articles/PMC3858429/ /pubmed/23925311 http://dx.doi.org/10.4161/rna.25273 Text en Copyright © 2013 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited. |
spellingShingle | Review Pinker, Franziska Bonnard, Géraldine Gobert, Anthony Gutmann, Bernard Hammani, Kamel Sauter, Claude Gegenheimer, Peter A Giegé, Philippe PPR proteins shed a new light on RNase P biology |
title | PPR proteins shed a new light on RNase P biology |
title_full | PPR proteins shed a new light on RNase P biology |
title_fullStr | PPR proteins shed a new light on RNase P biology |
title_full_unstemmed | PPR proteins shed a new light on RNase P biology |
title_short | PPR proteins shed a new light on RNase P biology |
title_sort | ppr proteins shed a new light on rnase p biology |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3858429/ https://www.ncbi.nlm.nih.gov/pubmed/23925311 http://dx.doi.org/10.4161/rna.25273 |
work_keys_str_mv | AT pinkerfranziska pprproteinsshedanewlightonrnasepbiology AT bonnardgeraldine pprproteinsshedanewlightonrnasepbiology AT gobertanthony pprproteinsshedanewlightonrnasepbiology AT gutmannbernard pprproteinsshedanewlightonrnasepbiology AT hammanikamel pprproteinsshedanewlightonrnasepbiology AT sauterclaude pprproteinsshedanewlightonrnasepbiology AT gegenheimerpetera pprproteinsshedanewlightonrnasepbiology AT giegephilippe pprproteinsshedanewlightonrnasepbiology |