Overproduction, purification and characterisation of Tbj1, a novel Type III Hsp40 from Trypanosoma brucei, the African sleeping sickness parasite

Full text for this resource is not available from the Research Repository.

Louw, Cassandra A, Ludewig, Michael H and Blatch, Gregory L (2010) Overproduction, purification and characterisation of Tbj1, a novel Type III Hsp40 from Trypanosoma brucei, the African sleeping sickness parasite. Protein Expression and Purification, 69 (2). pp. 168-177. ISSN 1046-5928

Abstract

The heat shock protein 40 (Hsp40) family of proteins act as co-chaperones of the heat shock protein 70 (Hsp70) chaperone family, and together they play a vital role in the maintenance of cellular homeostasis. The Type III class of Hsp40s are diverse in terms of both sequence identity and function and have not been extensively characterised. The Trypanosoma brucei parasite is the causative agent of Human African Trypanosomiasis, and possesses an unusually large Hsp40 complement, consisting mostly of Type III Hsp40s. A novel T. brucei Type III Hsp40, Tbj1, was heterologously expressed, purified, and found to exist as a compact monomer in solution. Using polyclonal antibodies to the full-length recombinant protein, Tbj1 was found by Western analysis to be expressed in the T. brucei bloodstream-form. Tbj1 was found to be able to assist two different Hsp70 proteins in the suppression of protein aggregation in vitro, despite being unable to stimulate their ATPase activity. This indicated that while Tbj1 did not possess independent chaperone activity, it potentially functioned as a novel co-chaperone of Hsp70 in T. brucei.

Dimensions Badge

Altmetric Badge

Item type Article
URI https://vuir.vu.edu.au/id/eprint/8135
DOI https://doi.org/10.1016/j.pep.2009.09.023
Official URL http://dx.doi.org/10.1016/j.pep.2009.09.023
Subjects Historical > Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
Historical > FOR Classification > 1101 Medical Biochemistry and Metabolomics
Keywords ResPubID22189, Hsp40, J-domain, T. brucei, ATPase, aggregation suppression
Citations in Scopus 8 - View on Scopus
Download/View statistics View download statistics for this item

Search Google Scholar

Repository staff login