Overexpression, purification and characterisation of the Plasmodium falciparum Hsp70-z (PfHsp70-z) protein.
Public Library of Science.
Six Hsp70-like genes are represented on the genome of Plasmodium falciparum. Of these two occur i0n the cytosol: P. falciparum Hsp70-z (PfHsp70-z) and PfHsp70-1. PfHsp70-1 is a well characterised canonical Hsp70 that facilitates protein quality control and is crucial for the development of malaria parasites. There is very little known about PfHsp70-z. However, PfHsp70-z is known to be essential and is implicated in suppressing aggregation of asparagine-rich proteins of P. falciparum. In addition, its expression at the clinical stage of malaria correlates with disease prognosis. Based on structural evidence PfHsp70-z belongs to the Hsp110 family of proteins. Since Hsp110 proteins have been described as nucleotide exchange factors (NEFs) of their canonical Hsp70 counterparts, it has been speculated that PfHsp70-z may serve as a NEF of PfHsp70-1. In the current study, P. falciparum cells cultured in vitro were subjected to heat stress, triggering the enhanced expression of PfHsp70-z. Biochemical assays conducted using recombinant PfHsp70-z protein demonstrated that the protein is heat stable and possesses ATPase activity. Furthermore, we observed that PfHsp70-z is capable of self-association. The structural-functional features of PfHsp70-z provide further evidence for its role as a chaperone and possible nucleotide exchange factor of PfHsp70-1.
adenosine triphosphatase; , chaperone; , heat shock protein 70; , controlled study; , cross reaction; , enzyme activity; , gene; , gene overexpression; , heat stress; , heat stress; , Hsp70 gene; , malaria; nonhuman; , Plasmodium falciparum; , protein aggregation; , protein expression; , protein purification; , protein secondary structure; , structure analysis; , temperature; , upregulation , Plasmodium falciparum;
Zininga, T. et al. 2015. Overexpression, purification and characterisation of the Plasmodium falciparum Hsp70-z (PfHsp70-z) protein. PLOS ONE 10(6):e0129445