par Flahaut, Sigrid ;Frère, J.;Boutibonnes, P.;Auffray, Y.
Référence Journal of basic microbiology, 37, 4, page (251-258)
Publication Publié, 1997
Référence Journal of basic microbiology, 37, 4, page (251-258)
Publication Publié, 1997
Article révisé par les pairs
Résumé : | Relationship between intrinsic thermal resistance, thermotolerance and heat shock proteins (hsp) synthesis is studied in Enterococcus faecalis. We showed that an impressive phenotypic heat resistance was induced by mild heat and a slight thermotolerance was developed by various sublethal pretreatments such as NaCl, SDS and bile salts. Hydrogen peroxide, acid and alkalin shifts or ‘thermomimetic’ agent such as ethanol, did not enhance the survival of adapted cells against the lethal thermal shock (62 °C). The inhibition of protein synthesis by chloramphenicol or rifampin abolished thermotolerance. The immunological identification of the DnaK and GroEL proteins in E. faecalis allowed to study induction of these molecular chaperones under various conditions. Heat was the most efficient inductor of DnaK and GroEL synthesis. However, it was surprising that ethanol did not strongly induce these proteins. We also show that amplification of these hsp is not correlated to acquired thermotolerance with a linear relationship. A weak thermotolerance is not coupled from increased synthesis of DnaK and GroEL. So, we postulate that the high synthesis of the major hsp is not obligatory in the thermal cross-protection but that de novo protein synthesis is an absolute necessity in E. faecalis. Activation of preformed hsp or other factors depending or not on protein synthesis may be also necessary to enhance thermal resistance. |