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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°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.

Original publication

DOI

10.1016/0014-5793(85)80373-2

Type

Journal article

Journal

FEBS Letters

Publisher

Wiley

Publication Date

02/09/1985

Volume

188

Pages

209 - 214