Stress proteins and cross-protection by heat shock and salt stress in Bacillus subtilis

Author: Volker, U.; Mach, H.; Schmid, R.; Hecker, M.

Description: Bacillus subtilis induced a set of general stress proteins in response to a salt or heat stress. Cells subjected to a mild heat stress showed a protective response which enabled them to survive otherwise lethal temperatures (e.g. 52 degrees C). In a similar way bacteria were enabled to survive toxic concentrations of NaCl by pretreatment with lower salt concentrations. A mild heat shock induced a cross-protection against lethal salt stress. The pretreatment of cells with low salt, however, was less effective in the induction of thermotolerance than a preceding mild heat stress. Three stress proteins were identified on the basis of their N-terminal amino acid sequences as homologues of GroEL, DnaK and ClpP of Escherichia coli. The role of general and specific stress proteins in the induction of thermotolerance/salt tolerance and cross-protection is discussed.

Subject headings: ATP-Dependent Proteases; Amino Acid Sequence; Bacillus subtilis; Bacterial Proteins; Cell Division; Chaperonin 60; Escherichia coli Proteins; HSP70 Heat-Shock Proteins; Heat-Shock Proteins; Hot Temperature; Molecular Sequence Data; Sequence Homology; Amino Acid; Serine Endopeptidases; Sodium Chloride; Salt; Stress

Publication year: 1992

Journal or book title: Journal of General Microbiology

Volume: 138

Issue: 10

Pages: 2125-2135

Find the full text: https://www.strategian.com/fulltext/Volker1992.pdf

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Serial number: 3597

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