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dc.contributor.author Botha, M
dc.contributor.author Chiang, AN
dc.contributor.author Needham, PG
dc.contributor.author Stephens, LL
dc.contributor.author Hoppe, HC
dc.contributor.author Külzer, S
dc.contributor.author Przyborski, JM
dc.contributor.author Lingelbach, K
dc.contributor.author Wipf, P
dc.contributor.author Brodsky, JL
dc.contributor.author Shonhai, A
dc.contributor.author Blatch, GL
dc.date.accessioned 2012-05-24T09:35:57Z
dc.date.available 2012-05-24T09:35:57Z
dc.date.issued 2011-07
dc.identifier.citation Botha, M, Chiang, AN, Needham, PG, Stephens, LL, Hoppe, HC, Külzer, S, Przyborski, JM, Lingelbach, K, Wipf, P, Brodsky, JL, Shonhai, A and Blatch, GL. 2011. Plasmodium falciparum encodes a single cytosolic type I Hsp40 that functionally interacts with Hsp70 and is upregulated by heat shock. Cell Stress and Chaperones, vol. 16(4), pp 389-401 en_US
dc.identifier.issn 1355-8145
dc.identifier.uri http://www.springerlink.com/content/k0q7936822165001/
dc.identifier.uri http://dx.doi.org/10.1007/s12192-010-0250-6
dc.identifier.uri http://hdl.handle.net/10204/5874
dc.description Copyright: 2010 Springer. This is the post-print version of the article. The definitive version is published in Cell Stress and Chaperones, vol. 16(4), pp 389-401 en_US
dc.description.abstract Heat shock protein 70 (Hsp70) and heat shock protein 40 (Hsp40) function as molecular chaperones during the folding and trafficking of proteins within most cell types. However, the Hsp70–Hsp40 chaperone partnerships within the malaria parasite, Plasmodium falciparum, have not been elucidated. Only one of the 43 P. falciparum Hsp40s is predicted to be a cytosolic, canonical Hsp40 (termed PfHsp40) capable of interacting with the major cytosolic P. falciparum-encoded Hsp70, PfHsp70. Consistent with this hypothesis, we found that PfHsp40 is upregulated under heat shock conditions in a similar pattern to PfHsp70. In addition, PfHsp70 and PfHsp40 reside mainly in the parasite cytosol, as assessed using indirect immunofluorescence microscopy. Recombinant PfHsp40 stimulated the ATP hydrolytic rates of both PfHsp70 and human Hsp70 similar to other canonical Hsp40s of yeast (Ydj1) and human (Hdj2) origin. In contrast, the Hsp40-stimulated plasmodial and human Hsp70 ATPase activities were differentially inhibited in the presence of pyrimidinone-based small molecule modulators. To further probe the chaperone properties of PfHsp40, protein aggregation suppression assays were conducted. PfHsp40 alone suppressed protein aggregation, and cooperated with PfHsp70 to suppress aggregation. Together, these data represent the first cellular and biochemical evidence for a PfHsp70–PfHsp40 partnership in the malaria parasite, and furthermore that the plasmodial and human Hsp70–Hsp40 chaperones possess unique attributes that are differentially modulated by small molecules. en_US
dc.language.iso en en_US
dc.publisher Springer en_US
dc.relation.ispartofseries Workflow;8979
dc.subject Aggregation en_US
dc.subject ATPase en_US
dc.subject Codon harmonisation en_US
dc.subject Heath shock protein en_US
dc.subject Malaria en_US
dc.subject Molecular chaperone en_US
dc.title Plasmodium falciparum encodes a single cytosolic type I Hsp40 that functionally interacts with Hsp70 and is upregulated by heat shock en_US
dc.type Article en_US


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