PFB0595w is a Plasmodium falciparum J protein that co-localizes with PfHsp70-1 and can stimulate its in vitro ATP hydrolysis activity

Heat shock proteins, many of which function as molecular chaperones, play important roles in the lifecycle and pathogenesis of the malaria parasite, Plasmodium falciparum. The P. falciparum heat shock protein 70 (PfHsp70) family of chaperones is potentially regulated by a large complement of J prote...

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Bibliographic Details
Published in:The international journal of biochemistry & cell biology 2015-05, Vol.62, p.47-53
Main Authors: Njunge, James M., Mandal, Pradipta, Przyborski, Jude M., Boshoff, Aileen, Pesce, Eva-Rachele, Blatch, Gregory L.
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - metabolism
Adenosine Triphosphate - metabolism
Chaperone
Cytosol - metabolism
DnaJ
Erythrocytes - parasitology
Hsp40
Hsp70
HSP72 Heat-Shock Proteins - metabolism
Humans
Hydrolysis
In Vitro Techniques
Malaria
Molecular Chaperones - metabolism
Plasmodium falciparum - cytology
Plasmodium falciparum - metabolism
Protein Binding
Protein Multimerization
Protozoan Proteins - metabolism
Tissue Distribution
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Summary:Heat shock proteins, many of which function as molecular chaperones, play important roles in the lifecycle and pathogenesis of the malaria parasite, Plasmodium falciparum. The P. falciparum heat shock protein 70 (PfHsp70) family of chaperones is potentially regulated by a large complement of J proteins that localize to various intracellular compartments including the infected erythrocyte cytosol. While PfHsp70-1 has been shown to be an abundant cytosolic chaperone, its regulation by J proteins is poorly understood. In this study, we characterized the J protein PFB0595w, a homologue of the well-studied yeast cytosolic J protein, Sis1. PFB0595w, similarly to PfHsp70-1, was localized to the parasite cytosol and its expression was upregulated by heat shock. Additionally, recombinant PFB0595w was shown to be dimeric and to stimulate the in vitro ATPase activity of PfHsp70-1. Overall, the expression, localization and biochemical data for PFB0595w suggest that it may function as a cochaperone of PfHsp70-1, and advances current knowledge on the chaperone machinery of the parasite.
ISSN:1357-2725
1878-5875
DOI:10.1016/j.biocel.2015.02.008