Comparative characterization of plasmodium falciparum Hsp70-1 relative to E. coli DnaK reveals the functional specificity of the parasite chaperone

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dc.contributor.authorLebepe, Charity Mekgwaen_ZA
dc.contributor.authorMatambanadzo, Pearl Rutendoen_ZA
dc.contributor.authorMakhoba, Xolani Henryen_ZA
dc.contributor.authorAchilonu, Ikechukwuen_ZA
dc.contributor.authorZininga, Tawandaen_ZA
dc.contributor.authorShonhai, Addmoreen_ZA
dc.date.accessioned2022-05-03T11:33:35Z
dc.date.available2022-05-03T11:33:35Z
dc.date.issued2020-06-04
dc.descriptionCITATION: Lebepe, Charity Mekgwa et al. 2020. Comparative characterization of plasmodium falciparum Hsp70-1 relative to E. coli DnaK reveals the functional specificity of the parasite chaperone. Biomolecules, 10(6): 856, doi:10.3390/biom10060856.en_ZA
dc.descriptionThe original publication is available at: https://www.ncbi.nlm.nih.goven_ZA
dc.description.abstractHsp70 is a conserved molecular chaperone. How Hsp70 exhibits specialized functions across species remains to be understood. Plasmodium falciparum Hsp70-1 (PfHsp70-1) and Escherichia coli DnaK are cytosol localized molecular chaperones that are important for the survival of these two organisms. In the current study, we investigated comparative structure-function features of PfHsp70-1 relative to DnaK and a chimeric protein, KPf, constituted by the ATPase domain of DnaK and the substrate binding domain (SBD) of PfHsp70-1. Recombinant forms of the three Hsp70s exhibited similar secondary and tertiary structural folds. However, compared to DnaK, both KPf and PfHsp70-1 were more stable to heat stress and exhibited higher basal ATPase activity. In addition, PfHsp70-1 preferentially bound to asparagine rich peptide substrates, as opposed to DnaK. Recombinant P. falciparum adenosylmethionine decarboxylase (PfAdoMetDC) co-expressed in E. coli with either KPf or PfHsp70-1 was produced as a fully folded product. Co-expression of PfAdoMetDC with heterologous DnaK in E. coli did not promote folding of the former. However, a combination of supplementary GroEL plus DnaK improved folding of PfAdoMetDC. These findings demonstrated that the SBD of PfHsp70-1 regulates several functional features of the protein and that this molecular chaperone is tailored to facilitate folding of plasmodial proteins.en_ZA
dc.description.versionPublisher's version
dc.format.extent21 pages : illustrationsen_ZA
dc.identifier.citationLebepe, Charity Mekgwa et al. 2020. Comparative characterization of plasmodium falciparum Hsp70-1 relative to E. coli DnaK reveals the functional specificity of the parasite chaperone. Biomolecules, 10(6): 856, doi:10.3390/biom10060856en_ZA
dc.identifier.otherdoi:10.3390/biom10060856
dc.identifier.urihttp://hdl.handle.net/10019.1/125177
dc.language.isoen_ZAen_ZA
dc.publisherMultidisciplinary Digital Publishing Institute (MDPI)
dc.rights.holderAuthors retain copyright
dc.subjectPlasmodium falciparum Hsp70-1en_ZA
dc.subjectMolecular chaperonesen_ZA
dc.subjectCo-expressionen_ZA
dc.subjectChaperone functionen_ZA
dc.subjectSpecificityen_ZA
dc.titleComparative characterization of plasmodium falciparum Hsp70-1 relative to E. coli DnaK reveals the functional specificity of the parasite chaperoneen_ZA
dc.typeArticleen_ZA
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