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

• DOI: 10.1016/j.biocel.2015.02.008
• Publication Date: 2015-02-18T01:04:17Z
• Authors: James M. Njunge; Pradipta Mandal; Jude M. Przyborski; Aileen Boshoff; Eva-Rachele Pesce; Gregory L. Blatch
• Keywords: 0301 basic medicine; 570; Erythrocytes; parasitology; College of Health and Biomedicine; Plasmodium falciparum; malaria; Protozoan Proteins; HSP72 Heat-Shock Proteins; To be catalogued; In Vitro Techniques; 0601 Biochemistry and Cell Biology; 03 medical and health sciences; Adenosine Triphosphate; Cytosol; chaperones; Humans; Tissue Distribution; Adenosine Triphosphatases; Hydrolysis; cytosolic; 3. Good health; PfHsp70-1; heat shock proteins; erythrocyte; Protein Multimerization; Molecular Chaperones; Protein Binding

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.