Projects per year
Abstract
Hsp40 proteins (also known as DnaJ or J proteins) serve as co-chaperones for Hsp70, but also display evidence of independent chaperone function. Furthermore, certain Hsp40s have been shown to be stress-inducible and essential. Trypanosomatids display a remarkable diversification of Hsp40 proteins, with numerous distinct Hsp40-like proteins encoded in the Trypanosoma brucei genome. This study investigated the role of one of the six T. brucei Type I Hsp40s, T. brucei J protein 2 (Tbj2). We found that Tbj2 was heat stress-inducible, and that knockdown using RNA interference resulted in a severe growth defect under normal growth temperatures. Furthermore, a green fluorescent protein (GFP)-Tbj2 fusion protein was found to be localized to the cytosol of T. brucei. Taken together, these data suggest that Tbj2 is not functionally equivalent to the other five Type I Hsp40s, and that it is an essential, cytosolic, and stress-inducible chaperone, potentially playing an important role in protein biogenesis in T. brucei.
Original language | English |
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Pages (from-to) | 93-98 |
Number of pages | 6 |
Journal | International Journal of Biochemistry and Cell Biology |
Volume | 60 |
Early online date | 3 Jan 2015 |
DOIs | |
Publication status | Published - Mar 2015 |
Keywords
- Hsp40
- Molecular chaperone
- RNA interference
- Tbj2
- Trypanosoma brucei
ASJC Scopus subject areas
- Biochemistry
- Cell Biology
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- 1 Finished
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High-Throughput Decoding of Virulence Mechanisms in African Trypanosomes (Senior Investigator Award)
Horn, D. (Investigator)
1/09/13 → 29/02/20
Project: Research