Molecular chaperones in biology, medicine and protein biotechnology

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Boshoff, Aileen, Nicoll, William S, Hennessy, Fritha, Ludewig, Michael H, Daniel, Sheryl, Modisakeng, Keoagile W, Shonhai, Addmore, McNamara, C, Bradley, Graeme and Blatch, Gregory ORCID: 0000-0003-0778-8577 (2004) Molecular chaperones in biology, medicine and protein biotechnology. South African Journal of Science, 100 (11-12). pp. 665-677. ISSN 0038-2353

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.

Additional Information

Online ISSN: 1996-7489

Item type Article
URI https://vuir.vu.edu.au/id/eprint/8163
Subjects Historical > Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
Historical > FOR Classification > 0601 Biochemistry and Cell Biology
Historical > FOR Classification > 0604 Genetics
Historical > FOR Classification > 1108 Medical Microbiology
Keywords ResPubID22218. molecular chaperones, proteins, DNA
Citations in Scopus 9 - View on Scopus
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