Molecular chaperones heat-shock proteins

Dutta D et al (2009) The molecular chaperone heat shock protein-90 positively regulates rotavims infectionx. Virology 391(2) 325—333... 

Molecular chaperone (relative molecular mass 78 K) found in the lumen of the ER. BiP is related to the Hsp70 family of heat-shock proteins and was originally described as immunoglobulin heavy chain binding protein. 

Molecular chaperones, stress proteins (note not all stress proteins are molecular chaperones and not all molecular chaperones are stress proteins) Heat shock proteins (Hsp) Polypeptide chain binding proteins... 

Hsp70 is a molecular chaperone (relative molecular mass 70 kD) found in different compartments of eucaryotic cells. Hsp70 was originally described as heat shock protein 70. 

Welch, W.J. (1991). The role of heat shock proteins as molecular chaperones Curr. Opin. Cell Biol. 3, 1033-1038. 

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. 

Powers, M.V. and Workman, P. (2006) Targeting of multiple signalling pathways by heat shock protein 90 molecular chaperone inhibitors. Endocrine-Related Cancer, 13 (Suppl. 1), S125-S135. 

Knittler MR, Dirks S, Haas IG (1995) Molecular chaperones involved in protein degradation in the endoplasmic reticulum quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum. Proc Natl Acad Sd USA 92 1764-1768... 

One group is the metallothioneins, which bind metals, another is the heat-shock proteins (hsps). These latter ones are called "molecular chaperones" and are involved in, for example,... 

Many of the chaperones double as heat shock-proteins (Hsp). When a cell is put under stress that can cause proteins to denature, such as too high a temperature, it produces heat-shock proteins. Their names are abbreviated to Hsp plus their subunit molecular mass in kDa. Hsp70, for example, is a ubiquitous heat-shock protein in eukaryotes. It is known in E. coli as DnaK for historical reasons because it was first discovered from a supposed role in DNA replication. Hsp70 is also important in protein trafficking and the conveying of proteins across membranes, because the denatured state is important in these processes. In protein biosynthesis, the unfolded state of the nascent polypeptide chain is passed on to DnaK, which maintains it in an extended form. The chain, under the influence of ATP and co-chaperones such as DnaJ and GrpE, is handed over to GroEL. 

Nagata K. Expression and function of heat shock protein 47 a collagen-specific molecular chaperone in the endoplasmic reticulum. Matrix Biology 1998, 16, 379-386. 

Georgopolous, C., and Welch, W. 1993. Role of major heat shock proteins as molecular chaperones. Annu. Rev. Cell Biol. 9 601-635. 

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. 

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