The pattern of protein synthesis induced by heat-shock of the moderately halophilic bacterium Chromobacterium marismortui: protective effect of high salt concentration against the thermal shock.
The protein synthetic response to heat shock of the moderately halophilic bacterium Chromobacterium marismortui was examined. Upon exposure to elevated temperature there is an increased synthesis of a specific subset of proteins (heat shock proteins-hsps) in the molecular weight region of 15 to 90 kD, while normal protein synthesis is severely repressed. The synthesis of hsps reaches a maximum 5 min after heat shock at 42 degrees C. Cells recovered their normal protein synthesis patterns rapidly upon returning to their normal growth temperature following heat shock. When cells grown in 2.5M NaCl were challenged with heat shock at 42 degrees C, the synthesis of some normal proteins was permitted. Furthermore, growth in high salt concentration resulted in an extension of the upper temperature limits at which C. marismortui could synthesize hsps. Adaptation of C. marismortui to decreasing salinity stimulated the synthesis of new proteins distinct from the hsps.
Katinakis
P
P
Aristotelian University of Thessaloniki, School of Science, Department of Biology, Greece.
D001426:Bacterial Proteins / Q000096:biosynthesis*; D002861:Chromobacterium / Q000187:drug effects / Q000378:metabolism*; D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel; D006360:Heat-Shock Proteins / Q000096:biosynthesis*; D006358:Hot Temperature; D008970:Molecular Weight; D012965:Sodium Chloride / Q000494:pharmacology*
D001426:Bacterial Proteins; D003470:Culture Media; D006360:Heat-Shock Proteins; D012965:Sodium Chloride