- Title
- Trypanosoma brucei J protein 2 is a stress inducible and essential Hsp40
- Creator
- Ludewig, Michael H
- Creator
- Boshoff, Aileen
- Creator
- Horn, David
- Creator
- Blatch, Gregory L
- Subject
- To be catalogued
- Date Issued
- 2015
- Date
- 2015
- Type
- text
- Type
- article
- Identifier
- http://hdl.handle.net/10962/431798
- Identifier
- vital:72804
- Identifier
- xlink:href="https://doi.org/10.1016/j.biocel.2014.12.016"
- Description
- 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.
- Format
- computer
- Format
- online resource
- Format
- application/pdf
- Format
- 1 online resource (6 pages)
- Format
- Publisher
- Elsevier
- Language
- English
- Relation
- The International Journal of Biochemistry and Cell Biology
- Relation
- Ludewig, M.H., Boshoff, A., Horn, D. and Blatch, G.L., 2015. Trypanosoma brucei J protein 2 is a stress inducible and essential Hsp40. The International Journal of Biochemistry and Cell Biology, 60, pp.93-98
- Relation
- The International Journal of Biochemistry and Cell Biology volume 60 p. 93 2015 1878-5875
- Rights
- Publisher
- Rights
- Use of this resource is governed by the terms and conditions of the Elsevier Terms and Conditions Statement (https://www.elsevier.com/legal/elsevier-website-terms-and-conditions)
- Rights
- Closed Access
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