Heat-shock proteins during growth and sporulation of Bacillus subtilis.
Four major heat-shock proteins (hsps) with apparent molecular masses of 84, 69, 32 and 22 kDa were detected in exponentially growing stationary phase and sporulating cells of Bacillus subtilis heat-shocked from 30 to 43 degrees C. The most abundant, hsp69, is probably analogous to the E. coli groEL protein. These proteins were transiently inducible by heat-shock. Partial purification of RNA polymerase revealed several other minor hsps. One of these, a 48 kDa polypeptide probably corresponds to sigma 43. The synthesis of this polypeptide and at least two other proteins appeared to be under sporulation and heat-shock regulation and was affected by the SpoOA mutation.
D001412:Bacillus subtilis / Q000254:growth & development / Q000378:metabolism* / Q000502:physiology; D001426:Bacterial Proteins / Q000378:metabolism*; D002846:Chromatography, Affinity; D012321:DNA-Directed RNA Polymerases / Q000502:physiology; D004591:Electrophoresis, Polyacrylamide Gel; D005786:Gene Expression Regulation; D006360:Heat-Shock Proteins / Q000378:metabolism*; D006493:Heparin / Q000378:metabolism; D011485:Protein Binding; D013171:Spores, Bacterial
D001426:Bacterial Proteins; D006360:Heat-Shock Proteins; D006493:Heparin; D012321:DNA-Directed RNA Polymerases