A Trypanosoma cruzi heat shock protein 40 is able to stimulate the adenosine triphosphate hydrolysis activity of heat shock protein 70 and can substitute for a yeast heat shock protein 40

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Edkins, Adrienne L, Ludewig, Michael H and Blatch, Gregory L (2004) A Trypanosoma cruzi heat shock protein 40 is able to stimulate the adenosine triphosphate hydrolysis activity of heat shock protein 70 and can substitute for a yeast heat shock protein 40. International Journal of Biochemistry and Cell Biology, 36 (8). pp. 1585-1598. ISSN 1357-2725

Abstract

The process of assisted protein folding, characteristic of members of the heat shock protein 70 (Hsp70) and heat shock protein 40 (Hsp40) molecular chaperone families, is important for maintaining the structural integrity of cellular protein machinery under normal and stressful conditions. Hsp70 and Hsp40 cooperate to bind non-native protein conformations in a process of adenosine triphosphate (ATP)-regulated assisted protein folding. We have analysed the molecular chaperone activity of the cytoplasmic inducible Hsp70 from Trypanosoma cruzi (TcHsp70) and its interactions with its potential partner Hsp40s (T. cruzi DnaJ protein 1 [Tcj1] and T. cruzi DnaJ protein 2 [Tcj2]). Histidine-tagged TcHsp70 (His-TcHsp70), Tcj1 (Tcj1-His) and Tcj2 (His-Tcj2) were over-produced in Escherichia coli and purified by nickel affinity chromatography. The in vitro basal specific ATP hydrolysis activity (ATPase activity) of His-TcHsp70 was determined as 40 nmol phosphate/min/mg protein, significantly higher than that reported for other Hsp70s. The basal specific ATPase activity was stimulated to a maximal level of 60 nmol phosphate/min/mg protein in the presence of His-Tcj2 and a model substrate, reduced carboxymethylated α-lactalbumin. In vivo complementation assays showed that Tcj2 was able to overcome the temperature sensitivity of the ydj1 mutant Saccharomyces cerevisiae strain JJ160, suggesting that Tcj2 may be functionally equivalent to the yeast Hsp40 homologue (yeast DnaJ protein 1, Ydj1). These data suggest that Tcj2 is involved in cytoprotection in a similar fashion to Ydj1, and that TcHsp70 and Tcj2 may interact in a nucleotide-regulated process of chaperone-assisted protein folding.

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Additional Information

Online ISSN: 1878-5875

Item type Article
URI https://vuir.vu.edu.au/id/eprint/8166
DOI https://doi.org/10.1016/j.biocel.2004.01.016
Official URL http://dx.doi.org/10.1016/j.biocel.2004.01.016
Subjects Historical > Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
Current > FOR Classification > 0601 Biochemistry and Cell Biology
Current > FOR Classification > 0604 Genetics
Keywords ResPubID22221. Hsp70, Hsp40, DnaJ, Trypanosoma cruzi, ATPase activity, reduced carboxymethylated alpha-lactalbumin, RCMLA, yeast complementation, heat shock protein
Citations in Scopus 25 - View on Scopus
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