Transcription of the apicoplast genome

Nisbet, R. Ellen R.; McKenzie, Jason

doi:10.1016/j.molbiopara.2016.07.004

Cited by 19 publications

(22 citation statements)

References 56 publications

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“…These transcripts are processed into individual mRNA, tRNA, and rRNA molecules often involving cleavage at the same UUAU motif. This motif is often found immediately adjacent to tRNA molecules (Nisbet et al, ; Nisbet & McKenzie, ).…”

Section: Discussionmentioning

confidence: 99%

“…The apicoplast genome encodes 30 proteins, two rRNAs, and 25 tRNAs (Wilson et al, ). Primary RNA transcripts are polycistronic, and there is extensive RNA processing to produce individual tRNA, rRNA, and mRNA molecules (Nisbet, Kurniawan, Bowers, & Howe, ; Nisbet & McKenzie, ). RNA processing must be controlled by nuclear‐encoded proteins that are targeted to the organelle, because no RNA processing proteins are encoded on the apicoplast genome.…”

Section: Introductionmentioning

confidence: 99%

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An essential pentatricopeptide repeat protein in the apicomplexan remnant chloroplast

Hicks

Lassadi

Carpenter

et al. 2019

Cellular Microbiology

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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.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

An essential pentatricopeptide repeat protein in the apicomplexan remnant chloroplast

Hicks

Lassadi

Carpenter

et al. 2019

Cellular Microbiology

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“…This apicoplast lost the ability to perform photosynthesis, however, is an essential organelle, and its inhibition is lethal. The apicoplast arose from a secondary endosymbiosis event occurred where an ancestor to Plasmodium engulfed a photosynthetic alga [24][25][26]. This organelle is involved in critical metabolic pathways such as the biosynthesis of fatty acids and heme group degradation [27,28].…”

Section: Apicoplast Genomementioning

confidence: 99%

“…The apicoplast genome is ~35 kbp smaller than chloroplasts due to the absence of genes encoding proteins involved in photosynthesis. The genome of this plastid has been reduced and contains ribosomal (rRNA) and transfer RNA (tRNA) genes that play an important role in organelle replication [24]. The characteristics of the structure of apicoplast genomes have difficult comparisons with other plastids [20].…”

Section: Apicoplast Genomementioning

confidence: 99%

Genomics of Apicomplexa

Martínez-Ocampo¹

2018

Farm Animals Diseases, Recent Omic Trends and New Strategies of Treatment

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Apicomplexa is a eukaryotic phylum of intracellular parasites with more than 6000 species. Some of these single-celled parasites are important pathogens of livestock. At present, 128 genomes of phylum Apicomplexa have been reported in the GenBank database, of which 17 genomes belong to five genera that are pathogens of farm animals: Babesia, Theileria, Eimeria, Neospora and Sarcocystis. These 17 genomes are Babesia bigemina (five chromosomes), Babesia divergens (514 contigs) and Babesia bovis (four chromosomes and one apicoplast); Theileria parva (four chromosomes and one apicoplast), Theileria annulata (four chromosomes), Theileria orientalis (four chromosomes and one apicoplast) and Theileria equi (four chromosomes and one apicoplast); Eimeria brunetti (24,647 contigs), Eimeria necatrix (4667 contigs), Eimeria tenella (12,727 contigs), Eimeria acervulina (4947 contigs), Eimeria maxima (4570 contigs), Eimeria mitis (65,610 contigs) and Eimeria praecox (53,359 contigs); Neospora caninum (14 chromosomes); and Sarcocystis neurona strains SN1 (2862 contigs) and SN3 (3191 contigs). The study of these genomes allows us to understand their mechanisms of pathogenicity and identify genes that encode proteins as a possible vaccine antigen.

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“…Alignments of PPR1 show that the 21 protein is well conserved across Plasmodium species ( Figure S1). PfPPR2 was predicted to lack 22 both a signal peptide and a mitochondrial targeting sequence so its location is unknown, but is 23 unlikely to be apicoplast targeted. 7 To test for the presence of PPRs more broadly in the Apicomplexa we searched for homologues 1 in Toxoplasma and Cryptosporidium.…”

Section: A Single Apicoplast Ppr Protein Present In Both Plasmodium Amentioning

confidence: 99%

A Pentatricopeptide Repeat Protein in the Plasmodium apicoplast is essential and shows sequence-specific RNA binding

Hicks

Lassadi

Carpenter

et al. 2018

Preprint

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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. Little is known about the mechanism of post-transcriptional processing. In plant chloroplasts, post-transcriptional RNA processing is controlled by multiple pentatricopeptide repeat (PPR) proteins. Here, we present the biochemical characterisation of the single apicoplast-targeted PPR protein. Apicoplast PPR1 is essential, and binds specific RNA sequences corresponding with previously characterized RNA processing sites. We identify the specific binding motif of PPR1. In RNAse protection assays, PPR1 shields apicoplast transcripts from ribonuclease degradation. Our results show that apicoplast RNA processing is under the control of a single protein, thus presenting an Achilles’ heel for the development of new anti-malarial drugs.

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Transcription of the apicoplast genome

Abstract: Graphical abstract

Cited by 19 publications

References 56 publications

An essential pentatricopeptide repeat protein in the apicomplexan remnant chloroplast

An essential pentatricopeptide repeat protein in the apicomplexan remnant chloroplast

Genomics of Apicomplexa

A Pentatricopeptide Repeat Protein in the Plasmodium apicoplast is essential and shows sequence-specific RNA binding

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