Literature DB >> 2264523

Microbial stress proteins.

K Watson1.   

Abstract

There is general agreement that a function, perhaps the major function, of stress proteins under normal physiological conditions is to help assembly and disassembly of protein complexes and to catalyse protein-translocation processes. It remains unclear, however, as to what role these processes play in stressed cells. It could be that cells under stress produce abnormal, misfolded or otherwise damaged proteins and that increased synthesis of stress proteins is required to counter protein modifications. A role for stress proteins in recovery of cells from stress, as opposed to a role in helping cells to withstand a lethal stress, is thus suggested. The intracellular location of stress proteins, in the unstressed and stressed cell, is worthy of further studies. Members of the hsp70 family are associated with the cytosol, mitochondria and endoplasmic reticulum. There is evidence, particularly from studies on mammalian cells (Tanguay, 1985; Welch and Mizzen, 1988; Arrigo et al., 1988), that following stress hsps migrate to various cellular compartments and subsequently delocalize after stress. However, there is little comparable data from microbial systems for this phenomenon (e.g. Rossi and Lindquist, 1989). The question as to the role of stress proteins in the transient acquisition of thermotolerance remains to be answered. It is insufficient to equate the kinetics of stress-protein synthesis with acquisition of thermotolerance. Quantitative data on the amount of stress protein present at various times, including the recovery period, is required. The demonstration that microbial stress proteins are important antigenic determinants of micro-organisms causing major debilitating diseases in the world is an exciting observation. Studies on the interplay of pathogen and host, both carrying similar antigenic hsp determinants, will be a challenging area for future research. It is likely that E. coli and Sacch. cerevisiae, with their well-established biochemical and genetic properties, will continue to be the experimental systems of choice for studies on stress proteins. On the other hand, it is encouraging that studies on other micro-organisms have expanded in the past few years and have made substantial contributions towards our understanding of the stress response. The ubiquitous nature of the stress response and the remarkable evolutionary conservation of the stress proteins continue to be attractive areas for research.

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Year:  1990        PMID: 2264523     DOI: 10.1016/s0065-2911(08)60122-8

Source DB:  PubMed          Journal:  Adv Microb Physiol        ISSN: 0065-2911            Impact factor:   3.517


  29 in total

1.  The origin of life--did it occur at high temperatures?

Authors:  S L Miller; A Lazcano
Journal:  J Mol Evol       Date:  1995       Impact factor: 2.395

2.  The involvement of transcriptional read-through from internal promoters in the expression of a novel endoglucanase gene FSendA, from Fibrobacter succinogenes AR1.

Authors:  R Cavicchioli; K Watson
Journal:  Nucleic Acids Res       Date:  1991-04-11       Impact factor: 16.971

3.  Cold shock and cold acclimation proteins in the psychrotrophic bacterium Arthrobacter globiformis SI55.

Authors:  F Berger; N Morellet; F Menu; P Potier
Journal:  J Bacteriol       Date:  1996-06       Impact factor: 3.490

4.  Molecular characterization of the Bacillus stearothermophilus PV72 S-layer gene sbsB induced by oxidative stress.

Authors:  B Kuen; A Koch; E Asenbauer; M Sará; W Lubitz
Journal:  J Bacteriol       Date:  1997-03       Impact factor: 3.490

5.  Influence of pH, Oxygen, and Humic Substances on Ability of Sunlight To Damage Fecal Coliforms in Waste Stabilization Pond Water.

Authors:  T P Curtis; D D Mara; S A Silva
Journal:  Appl Environ Microbiol       Date:  1992-04       Impact factor: 4.792

6.  Anti-Hsp65 antibodies recognize M proteins of group A streptococci.

Authors:  A Quinn; T M Shinnick; M W Cunningham
Journal:  Infect Immun       Date:  1996-03       Impact factor: 3.441

7.  Heat shock response in the thermophilic enteric yeast Arxiozyma telluris.

Authors:  M L Deegenaars; K Watson
Journal:  Appl Environ Microbiol       Date:  1998-08       Impact factor: 4.792

8.  The L-isoaspartyl protein repair methyltransferase enhances survival of aging Escherichia coli subjected to secondary environmental stresses.

Authors:  J E Visick; H Cai; S Clarke
Journal:  J Bacteriol       Date:  1998-05       Impact factor: 3.490

9.  Characterization of an acidic-pH-inducible stress protein (hsp70), a putative sulfatide binding adhesin, from Helicobacter pylori.

Authors:  M Huesca; A Goodwin; A Bhagwansingh; P Hoffman; C A Lingwood
Journal:  Infect Immun       Date:  1998-09       Impact factor: 3.441

10.  Polyubiquitin gene expression contributes to oxidative stress resistance in respiratory yeast (Saccharomyces cerevisiae).

Authors:  L Cheng; R Watt; P W Piper
Journal:  Mol Gen Genet       Date:  1994-05-10
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