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Feder, M. E., & Hofmann, G. E. (1999). Heat-shock proteins, molecular chaperones, and the stress response: Evolutionary and ecological physiology. Annual Review of Physiology, 61, 243–282. Added by: Dr. Enrique Feoli (30/04/2023, 18:32) Last edited by: Dr. Enrique Feoli (30/04/2023, 18:33) |
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| Resource type: Journal Article DOI: 10.1146/annurev.physiol.61.1.243 ID no. (ISBN etc.): 0066-4278 BibTeX citation key: Feder1999 View all bibliographic details  |
Categories: BioAcyl Corp Subcategories: Post-injury Regeneration Creators: Feder, Hofmann Collection: Annual Review of Physiology |
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| Abstract |
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Molecular chaperones, including the heat-shock proteins (Hsps), are a ubiquitous feature of cells in which these proteins cope with stress-induced denaturation of other proteins. Hsps have received the most attention in model organisms undergoing experimental stress in the laboratory, and the function of Hsps at the molecular and cellular level is becoming well understood in this context. A complementary focus is now emerging on the Hsps of both model and nonmodel organisms undergoing stress in nature, on the roles of Hsps in the stress physiology of whole multicellular eukaryotes and the tissues and organs they comprise, and on the ecological and evolutionary correlates of variation in Hsps and the genes that encode them. This focus discloses that (a) expression of Hsps can occur in nature, (b) all species have hsp genes but they vary in the patterns of their expression, (c) Hsp expression can be correlated with resistance to stress, and (d) species' thresholds for Hsp expression are correlated with levels of stress that they naturally undergo. These conclusions are now well established and may require little additional confirmation; many significant questions remain unanswered concerning both the mechanisms of Hsp-mediated stress tolerance at the organismal level and the evolutionary mechanisms that have diversified the hsp genes.
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