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Open AccessArticle

Comparative Characterization of Plasmodium falciparum Hsp70-1 Relative to E. coli DnaK Reveals the Functional Specificity of the Parasite Chaperone

1
Department of Biochemistry, School of Mathematical & Natural Sciences, University of Venda, Thohoyandou 0950, South Africa
2
Department of Biochemistry, Genetics and Microbiology, University of Pretoria, Pretoria 0028, South Africa
3
Protein Structure-Function Research Unit, School of Molecular and Cell Biology, University of the Witwatersrand, Johannesburg 2050, South Africa
4
Department of Biochemistry, Stellenbosch University, Stellenbosch 7602, South Africa
*
Author to whom correspondence should be addressed.
Biomolecules 2020, 10(6), 856; https://doi.org/10.3390/biom10060856
Received: 29 April 2020 / Revised: 21 May 2020 / Accepted: 1 June 2020 / Published: 4 June 2020
Hsp70 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. View Full-Text
Keywords: Plasmodium falciparum; Hsp70; co-expression; chaperone function; specificity Plasmodium falciparum; Hsp70; co-expression; chaperone function; specificity
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MDPI and ACS Style

Lebepe, C.M.; Matambanadzo, P.R.; Makhoba, X.H.; Achilonu, I.; Zininga, T.; Shonhai, A. Comparative Characterization of Plasmodium falciparum Hsp70-1 Relative to E. coli DnaK Reveals the Functional Specificity of the Parasite Chaperone. Biomolecules 2020, 10, 856. https://doi.org/10.3390/biom10060856

AMA Style

Lebepe CM, Matambanadzo PR, Makhoba XH, Achilonu I, Zininga T, Shonhai A. Comparative Characterization of Plasmodium falciparum Hsp70-1 Relative to E. coli DnaK Reveals the Functional Specificity of the Parasite Chaperone. Biomolecules. 2020; 10(6):856. https://doi.org/10.3390/biom10060856

Chicago/Turabian Style

Lebepe, Charity M.; Matambanadzo, Pearl R.; Makhoba, Xolani H.; Achilonu, Ikechukwu; Zininga, Tawanda; Shonhai, Addmore. 2020. "Comparative Characterization of Plasmodium falciparum Hsp70-1 Relative to E. coli DnaK Reveals the Functional Specificity of the Parasite Chaperone" Biomolecules 10, no. 6: 856. https://doi.org/10.3390/biom10060856

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