Stress proteins functions

Kwint K, Nachin L, Diez A, Nystrom T (2003). The bacterial universal stress protein Function and regulation. Curr. Opin. Microbiol. 6 140-145. 

Very large Serine/Threonine kinases and the molecular Target of Rapamycin, a naturally occurring secondary metabolite, TOR proteins function within multiprotein complexes to couple cell growth and stress responses to environmental and developmental cues. 

Pelham, H.R.B. (1990). Functions of the hsp70 protein family An overview. In Stress Proteins in Biology Medicine (Morimoto, R., Tissieres, A., Georgopoulos, C., eds.), pp. 287-300, CSHL Press, Cold Spring Harbor. 

Most of the stress proteins discussed in this account have a role either in helping the plants survive, or in minimising the effectiveness of the stress agent. In helping plants survive under stress conditions, the stress proteins perform the following functions (1) maintenance of the basic metabolism in the stressed cell, e.g. the induction of ADH and some... 

Oxidant Stress, Bedox StaU and Protein Function... 

Rao, R. P, Yuan, C., Allegood, J. C. et al. 2007. Ceramide transfer protein function is essential for normal oxidative stress response and lifespan. Proc. Natl. Acad. Sci. U.S.A., 104(27) 11364—11369. 

Figure 3. Role of nonhistone protein acetylation in maintaining cellular homeostasis- mis-regulation and disease connection (a) Acetylation of nonhistone proteins are associated with active or repressed chromatin architecture as guided by suitable cellular signals for maintenance of gene expression. Misreg-ulation of HAT function leads to diseased state, where chromatin architecture is altered than under normal condition. In a parallel way the posttranslational modification status of these proteins may act as versatile tool to diagnose the various stages of disease manifestation e.g. probable involvement of acetylated NPMl modulating its stress response function can lead us to use it as a marker for various disease states, (b) Acetylation of nonhistone proteins in connection to diseases like Cancer, AIDS, Diabetes and others. (See Colour Plate 14.)...

The ligand binding or catalytic sites are the most relevant parts of a protein domain for the development of small molecules as modulators of protein function. There is evidence that proteins with conserved folds often also have their functional sites on the same topological location. In some cases a remarkable conservatism in functional sites can be observed. This is true for the example described later in this review on similarity of Cdc25A phosphatase, acetylcholinesterase (AChE) and 1 Ifl-hydroxysteroid dehydrogenases (1 l HSD) (Fig. 9). Nevertheless, it should be stressed that the correlation patterns of amino acid sequence, protein fold and protein function remain a matter of debate. Moreover, a vast number of specific functions can be carried out by the limited number of protein domains due to the high amino acid diversity of proteins with similar folds. " ... 

Neckers, L., E. Mimnaugh, and T. Schulte. The function of heat shock proteins in stress tolerance degradation and reactivation of damaged proteins. In "Stress Proteins", D.S. Lachtman, Editor. Springer-Verlag, Heidelberg. 1999a. 

Heat-shock protein is part of a repair mechanism which involves protection and repair of cells following cellular damage due to exposure to a wide variety of stressors. Heat-shock stress protein HSP 70 has the capability to restore the damaged proteins under adverse conditions. Significant increases in the H S P 70 may directly interfere with ongoing cellular processes or may alter the function of the cells, whereas alowto... 

The response of cells to stress (including ROS and reactive metabolites) includes the upregulation of synthesis of stress proteins, which play a role in cell survival and thus serve a protective function. These are at a low level in the normal cell but help to maintain cell homeostasis. 

Klatt P, Lamas S. 2000. Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress. Fur J Biochem 267 4928 4944. 

In addition to structural roles, it is becoming increasingly apparent that a major function of IFs is to regulate the activities of cell metabolism, by serving as scaffolding for the dynamic regulation of associated proteins such as enzymes, signaling adapter molecules, stress proteins, cell death receptors, and even the endocytic machinery. 

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