Research Repository

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

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

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

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.

Item Type: Article
Uncontrolled Keywords: ResPubID22189, Hsp40, J-domain, T. brucei, ATPase, aggregation suppression
Subjects: Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
FOR Classification > 1101 Medical Biochemistry and Metabolomics
Depositing User: VUIR
Date Deposited: 12 Jul 2012 05:58
Last Modified: 23 Mar 2015 05:15
URI: http://vuir.vu.edu.au/id/eprint/8135
DOI: https://doi.org/10.1016/j.pep.2009.09.023
ePrint Statistics: View download statistics for this item
Citations in Scopus: 8 - View on Scopus

Repository staff only

View Item View Item

Search Google Scholar