Heat shock stress in Bacteroides fragilis

Goodman, Heide J. K.; Strydom, Eldie; Woods, David R.

doi:10.1007/bf00491904

“…1, except that the cells were stressed with 0.1% (vol/vol) butanol (11 mM) (lanes marked with B at the bottom) instead of being stressed with a temperature upshift. Not all stresses elicit the de novo synthesis of the same set of stress proteins in a number of bacteria studied, e.g., Sallmonella typhimnurilm (38), Bacteroides fiagilis (14), and Zymomonas mobilis (27), where more than one independent group of stress responses occur. In C. acetobltyliunm, however, the three stresses tested induced similar proteins but to different degrees.…”

Section: Resultsmentioning

confidence: 99%

“…Caulobacter crescentus (13,35), Zymomonas mobilis (27), Methylophilus methylotrophus (48), and Bacteroides fragilis (14). During the sporulation stages of B. subtilis, major hsps at 84 and 69 kDa have been found to be analogous to the products of the E. coli dnaK and the groEL genes, respec-C,) a 0 tively (2).…”

Section: Resultsmentioning

confidence: 99%

“…20 heat shock proteins (hsps) are induced in response to temperature upshifts. These proteins are thought to participate in the cellular response (or adaptation) to stress, as many of them are also induced by exposure of bacterial cells to a variety of stresses, including alcohols (27, 48), oxygen or H,O, (11,14,30,36), toxic metals (46), alkaline shift (40), and other stresses (38). Some of the hsps are highly conserved among archaebacteria (12), eubacteria, and eucaryotes (4, 5).…”

mentioning

confidence: 99%

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Stress- and Growth Phase-Associated Proteins of Clostridium acetobutylicum

Terracciano

¹

,

Rapaport

²

,

Kashket

³

1988

Appl Environ Microbiol

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The response of Clostridium acetobutylicum ATCC 4259 to the stresses produced by a temperature upshift from 28°C to 45°C and by exposure of the organisms to 0.1% n -butanol or to air was examined by analysis of pulse-labeled proteins. The stress response was the induction of the synthesis of a number of proteins, some of which were elicited by the three forms of stress. Eleven heat shock proteins were identified by two-dimensional electrophoresis, as were two proteins whose synthesis was heat sensitive. In the absence of applied stress, the synthesis of four proteins was found to be associated with the growth phase in batch culture; three of these proteins had a higher rate of de novo synthesis when the cells entered the solvent production phase. One of the stress-induced proteins, hsp74, was partially purified an found to be immunologically related to Escherichia coli heat shock protein Dnak. The similarities of the proteins induced at the onset of solventogenesis and by stress suggest a relationship between the two processes.

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“…The exposure of procaryotic and eucaryotic organisms to high growth temperatures induces an increased synthesis of proteins referred to as heat shock-proteins [1][2][3][4][5][6][7][8][9][10][11]. The same set of heat-shock proteins is induced by a variety of stresses other than heat, including ethanol, nalidixic acid, UV irradiation, DNA gyrase inhibitors and viral infection [8].…”

Section: Introductionmentioning

confidence: 99%

Preferential synthesis of stress proteins in stationary Zymomonas mobilis cells

Michel

¹

,

Stárka

²

1987

FEMS Microbiology Letters

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Most of the stress proteins induced after exposure of Zymomonas mobilis to sublethal heat or ethanol shock were shown to be major cellular proteins even in unshocked bacteria. However, a new polypeptide (E 18.5) was detected only after thermal or alcoholic stress. The appearance of E 18.5 was shown to be unrelated to a degradation process but to depend on protein synthesis. Induction of E 18.5 synthesis was controlled at the transcription level and the same conclusion can be drawn for other stress proteins. When cells entered the stationary phase, most of the proteins synthesized were of the stress protein group, including E 18.5. It is suggested that stress proteins, particularly E 18.5, could play an important role in the physiology of Z. mobilis and that they could be directly or indirectly involved in the mechanism of ethanol tolerance.

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“…The exposure of procaryotic and eucaryotic organisms to high growth temperatures induces an increased synthesis of proteins referred to as heat shock-proteins [1][2][3][4][5][6][7][8][9][10][11]. The same set of heat-shock proteins is induced by a variety of stresses other than heat, including ethanol, nalidixic acid, UV irradiation, DNA gyrase inhibitors and viral infection [8].…”

Section: Introductionmentioning

confidence: 99%

Preferential synthesis of stress proteins in stationary Zymomonas mobilis cells

Michel

¹

1987

FEMS Microbiology Letters

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Most of the stress proteins induced after exposure of Zymomonas mobilis to sublethal heat or ethanol shock were shown to be major cellular proteins even in unshocked bacteria. However, a new polypeptide (E 18.5) was detected only after thermal or alcoholic stress. The appearance of E 18.5 was shown to be unrelated to a degradation process but to depend on protein synthesis. Induction of E 18.5 synthesis was controlled at the transcription level and the same conclusion can be drawn for other stress proteins. When cells entered the stationary phase, most of the proteins synthesized were of the stress protein group, including E 18.5. It is suggested that stress proteins, particularly E 18.5, could play an important role in the physiology of Z. mobilis and that they could be directly or indirectly involved in the mechanism of ethanol tolerance.

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Heat shock stress in Bacteroides fragilis

Cited by 8 publications

References 19 publications

Stress- and Growth Phase-Associated Proteins of Clostridium acetobutylicum

Stress- and Growth Phase-Associated Proteins of Clostridium acetobutylicum

Preferential synthesis of stress proteins in stationary Zymomonas mobilis cells

Preferential synthesis of stress proteins in stationary Zymomonas mobilis cells

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