Makumire S, Zininga T, Vahokoski J, Kursula I, Shonhai A (2020) Biophysical analysis of Plasmodium falciparum Hsp70-Hsp90 organising protein (PfHop) reveals a monomer that is characterised by folded segments connected by flexible linkers. PLoS ONE 15(4): e0226657. https://doi.org/10.1371/journal.pone.0226657
Biophysical analysis of Plasmodium falciparum Hsp70-Hsp90 organising protein (PfHop) reveals a monomer that is characterised by folded segments connected by flexible linkers
|Author:||Makumire, Stanley1; Zininga, Tawanda1,2; Vahokoski, Juha3;|
1Department of Biochemistry, School of Mathematical & Natural Sciences, University of Venda, Thohoyandou, South Africa
2Department of Biochemistry, Stellenbosch University, Stellenbosch, South Africa
3Department of Biomedicine, University of Bergen, Bergen, Norway
4Biocenter Oulu & Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland
|Online Access:||PDF Full Text (PDF, 1 MB)|
|Persistent link:|| http://urn.fi/urn:nbn:fi-fe2020070947193
Public Library of Science,
|Publish Date:|| 2020-07-09
Plasmodium falciparum causes the most lethal form of malaria. The cooperation of heat shock protein (Hsp) 70 and 90 is thought to facilitate folding of select group of cellular proteins that are crucial for cyto-protection and development of the parasites. Hsp70 and Hsp90 are brought into a functional complex that allows substrate exchange by stress inducible protein 1 (STI1), also known as Hsp70-Hsp90 organising protein (Hop). P. falciparum Hop (PfHop) co-localises and occurs in complex with the parasite cytosolic chaperones, PfHsp70‐1 and PfHsp90. Here, we characterised the structure of recombinant PfHop using synchrotron radiation circular dichroism (SRCD) and small-angle X-ray scattering. Structurally, PfHop is a monomeric, elongated but folded protein, in agreement with its predicted TPR domain structure. Using SRCD, we established that PfHop is unstable at temperatures higher than 40°C. This suggests that PfHop is less stable at elevated temperatures compared to its functional partner, PfHsp70‐1, that is reportedly stable at temperatures as high as 80°C. These findings contribute towards our understanding of the role of the Hop-mediated functional partnership between Hsp70 and Hsp90.
|Type of Publication:||
A1 Journal article – refereed
|Field of Science:||
1182 Biochemistry, cell and molecular biology
1. IK, Sigrid Jusélius Foundation; https://sigridjuselius.fi/en/ 2. AS, L1/402/14–1; Deutsche Forchungsgemeinshaft; https://www.validate-network.org/event/german-african-cooperation-projects-in-infectiology-dfg 3. AS; 75464; 92598; National Research Foundation/Department of Science & Innovation of South Africa; https://www.nrf.ac.za/ 3. TZ; 111989; National Research Foundation of South Africa; www.nrf.ac.za.
© 2020 Makumire et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.