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An FtsH protease is recruited to the mitochondrion of Plasmodium falciparum.
- Source :
-
PloS one [PLoS One] 2013 Sep 13; Vol. 8 (9), pp. e74408. Date of Electronic Publication: 2013 Sep 13 (Print Publication: 2013). - Publication Year :
- 2013
-
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.
- Subjects :
- Adenosine Triphosphate pharmacology
Animals
Cytokinesis drug effects
Escherichia coli metabolism
Fluorescent Antibody Technique
Membrane Proteins metabolism
Mitochondria drug effects
Parasites cytology
Parasites drug effects
Parasites enzymology
Peptide Hydrolases chemistry
Phylogeny
Plasmodium falciparum cytology
Plasmodium falciparum drug effects
Protein Processing, Post-Translational drug effects
Protein Structure, Quaternary
Protein Transport drug effects
Protozoan Proteins chemistry
Recombinant Proteins metabolism
Sequence Homology, Amino Acid
Zinc pharmacology
Mitochondria enzymology
Peptide Hydrolases metabolism
Plasmodium falciparum enzymology
Protozoan Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1932-6203
- Volume :
- 8
- Issue :
- 9
- Database :
- MEDLINE
- Journal :
- PloS one
- Publication Type :
- Academic Journal
- Accession number :
- 24058559
- Full Text :
- https://doi.org/10.1371/journal.pone.0074408