Heat‐shock proteins during growth and sporulation of Bacillus subtilis

Open Access
Publisher Website
Google Scholar
Abstract
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°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 σ43. 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.