Molecular chaperones in biology, medicine and protein biotechnology

Boshoff, A. and Nicoll, W.S. and Hennessy, F. and Ludewig, M.H. and Daniel, S. and Modisakeng, K.W. and Shonhai, A. and McNamara, C. and Bradley, G. and Blatch, G.L. (2004) Molecular chaperones in biology, medicine and protein biotechnology. South African Journal of Science, 100 (11 & 12). pp. 665-677. ISSN 0038-2353

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Abstract

Molecular chaperones consist of several highly conserved families of proteins, many of which consist of heat shock proteins. The primary function of molecular chaperones is to facilitate the folding or refolding of proteins, and therefore they play an important role in diverse cellular processes including protein synthesis, protein translocation, and the refolding or degradation of proteins after cell stress. Cells are often exposed to different stressors, resulting in protein misfolding and aggregation. It is now well established that the levels of certain molecular chaperones are elevated during stress to provide protection to the cell. The focus of this review is on the impact of molecular chaperones in biology, medicine and protein biotechnology, and thus covers both fundamental and applied aspects of chaperone biology. Attention is paid to the functions and applications of molecular chaperones from bacterial and eukaryotic cells, focusing on the heat shock proteins 90 (Hsp90), 70 (Hsp70) and 40 (Hsp40) classes of chaperones, respectively. The role of these classes of chaperones in human diseases is discussed, as well as the parts played by chaperones produced by the causative agents of malaria and trypanosomiasis. Recent advances have seen the application of chaperones in improving the yields of a particular target protein in recombinant protein production. The prospects for the targeted use of molecular chaperones for the over-production of recombinant proteins is critically reviewed, and current research on these chaperones at Rhodes University is also discussed.

Item Type:Article
Additional Information:Rhodes Centenary issue. Chaperone Research Group, Department of Biochemistry, Microbiology and Biotechnology
Uncontrolled Keywords:proteins, molecular chaperones, protein biotechnology
Subjects:Y Unknown > Subjects to be assigned
Divisions:Faculty > Faculty of Science > Biochemistry, Microbiology & Biotechnology
ID Code:134
Deposited By: Rhodes Library Archive Administrator
Deposited On:15 Nov 2005
Last Modified:06 Jan 2012 16:17
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