The clp chaperones and proteases of the human malaria parasite Plasmodium falciparum

El Bakkouri, Majida, Pow, Andre, Mulichak, Anne, Cheung, Kevin L. Y., Artz, Jennifer D., Amani, Mehrnaz, Fell, Stuart, de Koning-Ward, Tania F., Goodman, C. Dean, McFadden, Geoffrey I., Ortega, Joaquin, Hui, Raymond and Houry, Walid A. 2010, The clp chaperones and proteases of the human malaria parasite Plasmodium falciparum, Journal of molecular biology, vol. 404, no. 3, pp. 456-477.

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Title The clp chaperones and proteases of the human malaria parasite Plasmodium falciparum
Formatted title The clp chaperones and proteases of the human malaria parasite Plasmodium falciparum
Author(s) El Bakkouri, Majida
Pow, Andre
Mulichak, Anne
Cheung, Kevin L. Y.
Artz, Jennifer D.
Amani, Mehrnaz
Fell, Stuart
de Koning-Ward, Tania F.
Goodman, C. Dean
McFadden, Geoffrey I.
Ortega, Joaquin
Hui, Raymond
Houry, Walid A.
Journal name Journal of molecular biology
Volume number 404
Issue number 3
Start page 456
End page 477
Total pages 22
Publisher Elsevier
Place of publication Amsterdam, The Netherlands
Publication date 2010-12-03
ISSN 0022-2836
1089-8638
Keyword(s) plasmodium falciparum
apicoplast
PfClp ATPases
PfClp proteases
protein homeostasis
malaria
Summary The Clp chaperones and proteases play an important role in protein homeostasis in the cell. They are highly conserved across prokaryotes and found also in the mitochondria of eukaryotes and the chloroplasts of plants. They function mainly in the disaggregation, unfolding and degradation of native as well as misfolded proteins. Here, we provide a comprehensive analysis of the Clp chaperones and proteases in the human malaria parasite Plasmodium falciparum. The parasite contains four Clp ATPases, which we term PfClpB1, PfClpB2, PfClpC and PfClpM. One PfClpP, the proteolytic subunit, and one PfClpR, which is an inactive version of the protease, were also identified. Expression of all Clp chaperones and proteases was confirmed in blood-stage parasites. The proteins were localized to the apicoplast, a non-photosynthetic organelle that accommodates several important metabolic pathways in P. falciparum, with the exception of PfClpB2 (also known as Hsp101), which was found in the parasitophorous vacuole. Both PfClpP and PfClpR form mostly homoheptameric rings as observed by size-exclusion chromatography, analytical ultracentrifugation and electron microscopy. The X-ray structure of PfClpP showed the protein as a compacted tetradecamer similar to that observed for Streptococcus pneumoniae and Mycobacterium tuberculosis ClpPs. Our data suggest the presence of a ClpCRP complex in the apicoplast of P. falciparum.
Language eng
Field of Research 060108 Protein Trafficking
Socio Economic Objective 970106 Expanding Knowledge in the Biological Sciences
HERDC Research category C1 Refereed article in a scholarly journal
Copyright notice ©2010, Elsevier
Persistent URL http://hdl.handle.net/10536/DRO/DU:30031493

Document type: Journal Article
Collection: School of Medicine
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