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

J Gen Microbiol. 1992 Oct;138(10):2125-35. doi: 10.1099/00221287-138-10-2125.


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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Dependent Proteases
  • Amino Acid Sequence
  • Bacillus subtilis / drug effects
  • Bacillus subtilis / physiology*
  • Bacterial Proteins / analysis
  • Bacterial Proteins / metabolism*
  • Cell Division / drug effects
  • Chaperonin 60
  • Escherichia coli Proteins*
  • HSP70 Heat-Shock Proteins*
  • Heat-Shock Proteins / analysis
  • Heat-Shock Proteins / physiology*
  • Hot Temperature
  • Molecular Sequence Data
  • Sequence Homology, Amino Acid
  • Serine Endopeptidases / analysis
  • Sodium Chloride / pharmacology


  • Bacterial Proteins
  • Chaperonin 60
  • Escherichia coli Proteins
  • HSP70 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Sodium Chloride
  • ATP-Dependent Proteases
  • Serine Endopeptidases
  • dnaK protein, E coli