Pentatricopeptide Repeat Proteins in Trypanosoma brucei Funtion in Mitochondrial Ribosomes

M. Pusnik, Ian Small, L.K. Read, T. Fabbro, A. Schneider

Research output: Contribution to journalArticle

84 Citations (Scopus)

Abstract

The pentatricopeptide repeat (PPR), a degenerate 35-amino-acid motif, defines a novel eukaryotic protein family. Plants have 400 to 500 distinct PPR proteins, whereas other eukaryotes generally have fewer than 5. The few PPR proteins that have been studied have roles in organellar gene expression, probably via direct interaction with RNA. Here we show that the parasitic protozoan Trypanosoma brucei encodes 28 distinct PPR proteins, an extraordinarily high number for a nonplant organism. A comparative analysis shows that seven out of eight selected PPR proteins are mitochondrially localized and essential for oxidative phosphoryllation. Six of these are required for the stabilization of mitochondrial rRNAs and, like ribosomes, are associated with the mitochondrial membranes. Furthermore, one of the PPR proteins copurifies with the large subunit rRNA. Finally, ablation of all of the PPR proteins that were tested induces degradation of the other PPR proteins, indicating that they function in concert. Our results show that a significant number of trypanosomal PPR proteins are individually essential for the maintenance and/or biogenesis of mitochondrial rRNAs.
Original languageEnglish
Pages (from-to)6876-6888
JournalMolecular and Cellular Biology
Volume27
Issue number19
DOIs
Publication statusPublished - 2007

Fingerprint

Dive into the research topics of 'Pentatricopeptide Repeat Proteins in Trypanosoma brucei Funtion in Mitochondrial Ribosomes'. Together they form a unique fingerprint.

Cite this