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An essential pentatricopeptide repeat protein in the apicomplexan remnant chloroplast.

Accepted version
Peer-reviewed

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Authors

Hicks, Joanna L 
Lassadi, Imen 
Eno, Madeleine 
Vardakis, Alexandros 

Abstract

The malaria parasite Plasmodium and other apicomplexans such as Toxoplasma evolved from photosynthetic organisms and contain an essential, remnant plastid termed the apicoplast. Transcription of the apicoplast genome is polycistronic with extensive RNA processing. Yet little is known about the mechanism of apicoplast RNA processing. In plants, chloroplast RNA processing is controlled by multiple pentatricopeptide repeat (PPR) proteins. Here, we identify the single apicoplast PPR protein, PPR1. We show that the protein is essential and that it binds to RNA motifs corresponding with previously characterized processing sites. Additionally, PPR1 shields RNA transcripts from ribonuclease degradation. This is the first characterization of a PPR protein from a nonphotosynthetic plastid.

Description

Keywords

Plasmodium, RNA processing, Toxoplasma, apicomplexa, apicoplast, plastid, Apicoplasts, Chloroplasts, Phylogeny, Plasmodium falciparum, Toxoplasma

Journal Title

Cell Microbiol

Conference Name

Journal ISSN

1462-5814
1462-5822

Volume Title

21

Publisher

Hindawi Limited

Rights

All rights reserved
Sponsorship
Wellcome Trust (094249/Z/10/Z)
MRC (MC_PC_14116 v2)
Medical Research Council (MR/M011690/1)