Research Repository

Plasmodium falciparum Hep1 is required to prevent the self aggregation of PfHsp70-3

Nyakundi, DO, Vuko, LAM, Bentley, SJ, Hoppe, H, Blatch, Gregory ORCID: 0000-0003-0778-8577 and Boshoff, A (2016) Plasmodium falciparum Hep1 is required to prevent the self aggregation of PfHsp70-3. PLoS ONE, 11 (6). ISSN 1932-6203

[img] Text
file.pdf - Published Version
Available under License Creative Commons Attribution.

Download (1MB)


The majority of mitochondrial proteins are encoded in the nucleus and need to be imported from the cytosol into the mitochondria, and molecular chaperones play a key role in the efficient translocation and proper folding of these proteins in the matrix. One such molecular chaperone is the eukaryotic mitochondrial heat shock protein 70 (Hsp70); however, it is prone to self-aggregation and requires the presence of an essential zinc-finger protein, Hsp70-escort protein 1 (Hep1), to maintain its structure and function. PfHsp70-3, the only Hsp70 predicted to localize in the mitochondria of P. falciparum, may also rely on a Hep1 orthologue to prevent self-aggregation. In this study, we identified a putative Hep1 orthologue in P. falciparum and co-expression of PfHsp70-3 and PfHep1 enhanced the solubility of PfHsp70-3. PfHep1 suppressed the thermally induced aggregation of PfHsp70-3 but not the aggregation of malate dehydrogenase or citrate synthase, thus showing specificity for PfHsp70-3. Zinc ions were indeed essential for maintaining the function of PfHep1, as EDTA chelation abrogated its abilities to suppress the aggregation of PfHsp70-3. Soluble and functional PfHsp70-3, acquired by co-expression with PfHep-1, will facilitate the biochemical characterisation of this particular Hsp70 protein and its evaluation as a drug target for the treatment of malaria.

Item Type: Article
Uncontrolled Keywords: malaria treatment; cytosol; mitochondria; molecular chaperones; protein aggregation; Hsp70 protein; PfHep1
Subjects: Current > FOR Classification > 1101 Medical Biochemistry and Metabolomics
Current > Division/Research > College of Health and Biomedicine
Depositing User: Symplectic Elements
Date Deposited: 17 Sep 2017 23:36
Last Modified: 20 Sep 2017 03:35
ePrint Statistics: View download statistics for this item
Citations in Scopus: 3 - View on Scopus

Repository staff only

View Item View Item

Search Google Scholar