Is thermotolerance correlated to heat-shock protein synthesis in Lactococcus lactis subsp. lactis?
Exposure of Lactococcus lactis subsp. lactis cells to a heat shock at 40 degrees C for 30 min induces thermotolerance, the increased ability of bacterial cells to survive exposure to lethal temperature (52 degrees C for 25 min). This transient state of thermal resistance is accompanied, as in Escherichia coli, by the synthesis of a new set of specific proteins termed heat-shock proteins (Hsps). Pre-treatment of the bacterial cells by antibiotics (streptomycin, spiramycin, kanamycin and erythromycin) known to act on translation, induces the major Hsps synthesis but no thermal protection; conversely, puromycin and amino acid analogues treatments, known to produce abnormal and incomplete peptides, triggers the thermotolerance state without inducing significant Hsps synthesis. These results demonstrate that heat-shock response and induced thermotolerance are not tightly correlated phenomena in L. lactis subsp. lactis.
Boutibonnes
P
P
Laboratoire de Génétique Microbienne, I.R.B.A., Université de Caen, France.
Tranchard
C
C
Hartke
A
A
Thammavongs
B
B
Auffray
Y
Y
D000222:Adaptation, Physiological; D000596:Amino Acids / Q000494:pharmacology; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D006360:Heat-Shock Proteins / Q000096:biosynthesis* / Q000187:drug effects; D006358:Hot Temperature; D013294:Lactococcus lactis / Q000187:drug effects / Q000378:metabolism*; D013045:Species Specificity; D013997:Time Factors
D000596:Amino Acids; D000900:Anti-Bacterial Agents; D006360:Heat-Shock Proteins