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• W25269226 abstract "Cells respond to stresses such as elevated temperature, heavy metals, and amino acid analogs by inducing the transcription of a set of genes whose products, known as stress proteins, enhance survival under stress conditions. The major shared property of conditions and agents which induce the stress response is the ability to damage cellular proteins. Protein damage is a key event in the induction of the stress response, as indicated by the finding that forced production of denatured proteins triggers the synthesis of heat shock proteins at sub-heat shock temperatures (Goff and Goldberg 1985; Ananthan et al. 1986). Moreover, reducing intracellular levels of damaged proteins is a principal objective of the stress response, because protein damage can be highly toxic: the denaturation of a protein not only causes the loss of function of that specific molecule, but may also, through the improper exposure of hydrophobic amino acid side chains, lead to the aggregation of other proteins. Levels of damaged proteins can be reduced in two ways (Parsell and Lindquist 1993; Sherman and Goldberg 1996; Gottesman et al. 1997). On the one hand, specific molecular chaperones can prevent the aggregation of damaged proteins, and catalyze their refolding. On the other hand, specific proteases can degrade damaged proteins. These two strategies for coping with stress-denatured proteins, namely salvage and elimination, may not be fully independent. Nor are the essential functions of chaperones and proteases restricted to stress conditions." @default.
• W25269226 created "2016-06-24" @default.
• W25269226 creator A5074152513 @default.
• W25269226 date "1999-01-01" @default.
• W25269226 modified "2023-10-13" @default.
• W25269226 title "Ubiquitin and the Stress Response" @default.
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• W25269226 doi "https://doi.org/10.1007/978-3-642-58259-2_6" @default.
• W25269226 hasPublicationYear "1999" @default.
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