Chaperones heat-shock response molecular

Feder, M.E., and G.E. Hofmann (1999). Heat-shock proteins, molecular chaperones and the stress response Evolutionary and ecological physiology. Annu. Rev. Physiol. 61 243-282. 

In virtually all organisms, enhanced synthesis of heat shock proteins (HSPs) occurs in response to environmental, chemical, and physiological stresses. Some members of the evolutionarily conserved HSP gene family are constitutively expressed and function as molecular chaperones. It has been demonstrated that HSP induction results primarily from the activation of a heat shock transcription factor (HSF) with subsequent binding to heat shock response DNA elements (HSEs) in the enhancer regions of the HSP genes157. Heat shock responses in fish have been recently reviewed by Basu et al.15 and will be discussed in another chapter of this volume, so we will primarily limit our discussions to heat shock responses in zebrafish. 

Historically, efforts to characterize the cell s basal protein folding and degradation machinery have been spearheaded by the analysis of proteins specifically induced by the classic heat shock response. Yet it is clear that cellular responses to heat and other stresses that compromise protein folding encompass a range of biochemical activities far broader than molecular chaperones and proteases. The availability of complete genomic sequences from a range of eukaryotes, bacteria, and archae,... 

The previous section looked at examples in which detailed analysis of specific proteins identified as targets of the heat shock response has led to the identification of new molecular chaperones as well as an expanded view of the requirements for efficient protein production and folding. In this section we focus on how the use of DNA microarrays has provided a global view of the spectrum of targets of a specific stress response, the unfolded protein response (UPR), which plays a critical... 

Jolly C., Morimoto R.I., 2000, Role of the heat shock response and molecular chaperones in oncogenesis and cell death. J. Natl.CancerInst. 92 1564-1572. 

Many appear to act as chaperonins (see Molecular chaperones) in bacterial cells, the cytoplasm of eukaryotic cells, and mitochondria. The 1 70 family in i -ticular appears to chaperone the insertion of proteins into membranes. [O. Bensaude et al. Nature 305 (1983) 331-332 E. A. Craig The heat shock response CRC Cril. Rev. Biochem. 18 (1986) 239-280 CWu Heat Shock llanscription Factors Structure and Regulation Amu. Rev. Cell Dev. Biol. 11 (1995) 441-469]... 

Both the heat and cold shock response are universal and have been studied extensively. The major heat shock proteins (HSPs) are highly conserved. They are involved in the homeostatic adaptation of cells to harsh environmental conditions. Some act as molecular chaperones for protein folding, while others are involved in the processing of denatured polypeptides whose accumulation would be deleterious. The cold shock results in the transient induction of cold shock proteins (CSPs), which include a family of small acidic proteins carrying the cold shock domain. The CSPs appear to be involved in various cellular functions such as transcription, translation and DNA recombination. 

Heat shock proteins (HSPs) are a family of proteins expressed in almost all organisms from prokaryotes to humans. HSPs were originally described about four decades ago as proteins that were induced in the Drosophila melanogaster in response to a heat stress and hence derive the name HSR However, research over the years has uncovered these proteins to have a multitude of functions. Primarily, all HSPs act as molecular chaperons and assist in proper folding of naive proteins. Furthermore, HSPs have important roles in cellular processes including cell survival, inflammation, immunity, ion channel repair, and others. HSPs are also induced by a variety of stressors. Reactive oxygen species, cytotoxic injury, necrosis, ultraviolet radiation, metals, and many others are some examples. 

Wang, W., B. Vinocur, O. Shoseyov, and A. Altman. 2004. Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response. Trends Plant Sci. 9 244-252. 

Heat shock proteins (Hsp), stress-response proteins, a group of highly conserved proteins in both prokaryotes and eukaryotes, formed in response to hyperthermia or other noxious conditions. Almost all Hsp function as molecular chaperones. According to their molecular weight (in kDa), the Hsp are divided into six main families. (1) HsplOO belongs to the AAA + protein super family (adenosine triphosphatases with diverse activities) sharing a common... 

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