Article
Hsp70, an important cog in the malaria parasite’s protein folding machinery
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Published: | January 8, 2013 |
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Heat shock proteins (Hsps) play a central role as part of the cell’s molecular chaperone machinery. Hsp70s are proteins that are characterized by a highly conserved ATPase domain and a peptide binding domain (PBD). Hsp70 is capable of binding hydrophobic patches that are displayed by misfolded proteins. This allows it to stabilize unfolded proteins, facilitating their refolding. Plasmodium falciparum encodes 6 Hsp70s which are located in various cellular organelles. This report analyses the specialized roles of these proteins and discusses their central role in protein folding in the malaria parasite. Plasmodium falciparum Hsp70-1 (PfHsp70-1), is a stress-inducible cytosol/nuclear localized protein. Evidence for the chaperone role of this protein is presented. Furthermore, insights into its interaction with other molecular chaperones and co-chaperones such as PfHsp90, and Hsp40 co-chaperones will be discussed.