An essential pentatricopeptide repeat protein in the apicomplexan remnant chloroplast. (16th September 2019)

• Record Type: Journal Article
• Authors: Hicks, Joanna L.; Lassadi, Imen; Carpenter, Emma F.; Eno, Madeleine; Vardakis, Alexandros; Waller, Ross F.; Howe, Christopher J.; Nisbet, R. Ellen R.
• Is Part Of: Cellular microbiology. Volume 21:Number 12(2019)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2019-09-16
• Subjects: apicomplexa -- apicoplast -- Plasmodium -- plastid -- RNA processing -- Toxoplasma; Microbiology -- Periodicals; Cytology -- Periodicals; Host-parasite relationships -- Periodicals; Microbiology -- Periodicals; Cells -- Periodicals; Microbiologie -- Périodiques; Microbiologie; Relation hôte-parasite; Cytologie; Cellule; Réponse cellulaire; Ressource Internet (Descripteur de forme); Périodique électronique (Descripteur de forme); 579.05
• DOI: 10.1111/cmi.13108
• Languages: English
• ISSNs: 1462-5814

Abstract

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.