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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.


Journal article



Publication Date





209 - 214


Bacillus subtilis, Bacterial Proteins, Chromatography, Affinity, DNA-Directed RNA Polymerases, Electrophoresis, Polyacrylamide Gel, Gene Expression Regulation, Heat-Shock Proteins, Heparin, Protein Binding, Spores, Bacterial