ArticlePloS one2013
An FtsH protease is recruited to the mitochondrion of Plasmodium falciparum.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 24 citations in OpenAlex.
- Mitochondrial proteome of the apicomplexan Babesia divergens.Current biology : CB · 2026Article
- Identification of genetic markers of quinine partial resistance in Plasmodium falciparum.Nature microbiology · 2026Article
- ATAD3 megadalton complex in Plasmodium falciparum is essential for mitochondrial and cellular viability.PLoS pathogens · 2026Article
- A bacterial-type cardiolipin synthase in Plasmodium spp. supports mitochondrial respiration and is important for liver stage maturation.PLoS pathogens · 2026Article
- Plasmodium falciparum stomatin-like protein forms a putative complex with a metalloprotease in distinct mitochondrial loci.PLoS pathogens · 2026Article
- Orchestrating a heist: uptake and storage of metals by apicomplexan parasites.Microbiology (Reading, England) · 2021Article
- A single point mutation in theeLife · 2020Article
- Metallopeptidases of Toxoplasma gondii: in silico identification and gene expression.Parasite (Paris, France) · 2018Article
- Small molecule inhibition of apicomplexan FtsH1 disrupts plastid biogenesis in human pathogens.eLife · 2017Article
- Proteases as antimalarial targets: strategies for genetic, chemical, and therapeutic validation.The FEBS journal · 2017Review
- Sulfur mobilization for Fe-S cluster assembly by the essential SUF pathway in the Plasmodium falciparum apicoplast and its inhibition.Antimicrobial agents and chemotherapy · 2014Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The two organelles, apicoplast and mitochondrion, of the malaria parasite Plasmodium falciparum have unique morphology in liver and blood stages; they undergo complex branching and looping prior to division and segregation into daughter merozoites. Little is known about the molecular processes and proteins involved in organelle biogenesis in the parasite. We report the identification of an AAA+/FtsH protease homolog (PfFtsH1) that exhibits ATP- and Zn(2+)-dependent protease activity. PfFtsH1 undergoes processing, forms oligomeric assemblies, and is associated with the membrane fraction of the parasite cell. Generation of a transfectant parasite line with hemagglutinin-tagged PfFtsH1, and immunofluorescence assay with anti-PfFtsH1 Ab demonstrated that the protein localises to P. falciparum mitochondria. Phylogenetic analysis and the single transmembrane region identifiable in PfFtsH1 suggest that it is an i-AAA like inner mitochondrial membrane protein. Expression of PfFtsH1 in Escherichia coli converted a fraction of bacterial cells into division-defective filamentous forms implying a sequestering effect of the Plasmodium factor on the bacterial homolog, indicative of functional conservation with EcFtsH. These results identify a membrane-associated mitochondrial AAA+/FtsH protease as a candidate regulatory protein for organelle biogenesis in P. falciparum.
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