RAP proteins regulate apicoplast noncoding RNA processing in Plasmodium falciparum
Summary: The human malaria parasite, Plasmodium falciparum, contains a non-photosynthetic and essential plastid called the apicoplast. This organelle is of major interest for its unique biology and potential as an attractive drug target. In this study, we characterize PfRAP03 and PfRAP08, two member...
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| Format: | Article |
| Language: | English |
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Elsevier
2025-07-01
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| Series: | Cell Reports |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124725006990 |
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| author | Thomas Hollin Zeinab Chahine Steven Abel Charles Banks Charisse Flerida A. Pasaje Todd Lenz Jacques Prudhomme Caitlyn Marie Ybanez Anahita S. Abbaszadeh Jacquin C. Niles Laurence Florens Karine G. Le Roch |
| author_facet | Thomas Hollin Zeinab Chahine Steven Abel Charles Banks Charisse Flerida A. Pasaje Todd Lenz Jacques Prudhomme Caitlyn Marie Ybanez Anahita S. Abbaszadeh Jacquin C. Niles Laurence Florens Karine G. Le Roch |
| author_sort | Thomas Hollin |
| collection | DOAJ |
| description | Summary: The human malaria parasite, Plasmodium falciparum, contains a non-photosynthetic and essential plastid called the apicoplast. This organelle is of major interest for its unique biology and potential as an attractive drug target. In this study, we characterize PfRAP03 and PfRAP08, two members of the RAP (RNA-binding domain abundant in apicomplexans) protein family. We generate inducible knockdown lines in P. falciparum to validate that both RAP proteins are essential for parasite survival and localize to the apicoplast. Transcriptomic analysis demonstrates that PfRAP03 and PfRAP08 depletion significantly affect apicoplast gene expression. Using enhanced crosslinking immunoprecipitation sequencing (eCLIP-seq) method, we show that apicoplast ribosomal RNAs and transfer RNAs are the targets of PfRAP03 and PfRAP08, respectively. Collectively, our results establish the role of these RAP proteins in controlling apicoplast gene expression in P. falciparum, revealing parasite-specific organellar pathways with biomedical significance. |
| format | Article |
| id | doaj-art-c35a5eff52ba4f21bcb56cc843619d10 |
| institution | Kabale University |
| issn | 2211-1247 |
| language | English |
| publishDate | 2025-07-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Cell Reports |
| spelling | doaj-art-c35a5eff52ba4f21bcb56cc843619d102025-08-20T03:24:44ZengElsevierCell Reports2211-12472025-07-0144711592810.1016/j.celrep.2025.115928RAP proteins regulate apicoplast noncoding RNA processing in Plasmodium falciparumThomas Hollin0Zeinab Chahine1Steven Abel2Charles Banks3Charisse Flerida A. Pasaje4Todd Lenz5Jacques Prudhomme6Caitlyn Marie Ybanez7Anahita S. Abbaszadeh8Jacquin C. Niles9Laurence Florens10Karine G. Le Roch11Department of Molecular, Cell and Systems Biology, University of California, Riverside, Riverside, CA, USADepartment of Molecular, Cell and Systems Biology, University of California, Riverside, Riverside, CA, USADepartment of Molecular, Cell and Systems Biology, University of California, Riverside, Riverside, CA, USAStowers Institute for Medical Research, Kansas City, MO, USADepartment of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA, USADepartment of Molecular, Cell and Systems Biology, University of California, Riverside, Riverside, CA, USADepartment of Molecular, Cell and Systems Biology, University of California, Riverside, Riverside, CA, USADepartment of Molecular, Cell and Systems Biology, University of California, Riverside, Riverside, CA, USADepartment of Molecular, Cell and Systems Biology, University of California, Riverside, Riverside, CA, USADepartment of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA, USAStowers Institute for Medical Research, Kansas City, MO, USADepartment of Molecular, Cell and Systems Biology, University of California, Riverside, Riverside, CA, USA; Corresponding authorSummary: The human malaria parasite, Plasmodium falciparum, contains a non-photosynthetic and essential plastid called the apicoplast. This organelle is of major interest for its unique biology and potential as an attractive drug target. In this study, we characterize PfRAP03 and PfRAP08, two members of the RAP (RNA-binding domain abundant in apicomplexans) protein family. We generate inducible knockdown lines in P. falciparum to validate that both RAP proteins are essential for parasite survival and localize to the apicoplast. Transcriptomic analysis demonstrates that PfRAP03 and PfRAP08 depletion significantly affect apicoplast gene expression. Using enhanced crosslinking immunoprecipitation sequencing (eCLIP-seq) method, we show that apicoplast ribosomal RNAs and transfer RNAs are the targets of PfRAP03 and PfRAP08, respectively. Collectively, our results establish the role of these RAP proteins in controlling apicoplast gene expression in P. falciparum, revealing parasite-specific organellar pathways with biomedical significance.http://www.sciencedirect.com/science/article/pii/S2211124725006990CP: Microbiology |
| spellingShingle | Thomas Hollin Zeinab Chahine Steven Abel Charles Banks Charisse Flerida A. Pasaje Todd Lenz Jacques Prudhomme Caitlyn Marie Ybanez Anahita S. Abbaszadeh Jacquin C. Niles Laurence Florens Karine G. Le Roch RAP proteins regulate apicoplast noncoding RNA processing in Plasmodium falciparum Cell Reports CP: Microbiology |
| title | RAP proteins regulate apicoplast noncoding RNA processing in Plasmodium falciparum |
| title_full | RAP proteins regulate apicoplast noncoding RNA processing in Plasmodium falciparum |
| title_fullStr | RAP proteins regulate apicoplast noncoding RNA processing in Plasmodium falciparum |
| title_full_unstemmed | RAP proteins regulate apicoplast noncoding RNA processing in Plasmodium falciparum |
| title_short | RAP proteins regulate apicoplast noncoding RNA processing in Plasmodium falciparum |
| title_sort | rap proteins regulate apicoplast noncoding rna processing in plasmodium falciparum |
| topic | CP: Microbiology |
| url | http://www.sciencedirect.com/science/article/pii/S2211124725006990 |
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