Heat-shock proteins during growth and sporulation of Bacillus subtilis

• Published in: FEBS letters 1985-09, Vol.188 (2), p.209-214
• Main Authors: Todd, J.A., Hubbard, T.J.P., Travers, A.A., Ellar, D.J.
• Format: Article
• Language: English
• Subjects: Applied sciences; Bacillus subtilis; Bacillus subtilis - growth & development; Bacillus subtilis - metabolism; Bacillus subtilis - physiology; Bacterial Proteins - metabolism; Bacteriology; Biological and medical sciences; Chromatography, Affinity; DNA-Directed RNA Polymerases - physiology; Electrophoresis, Polyacrylamide Gel; Exact sciences and technology; Fundamental and applied biological sciences. Psychology; Gene Expression Regulation; Growth, nutrition, cell differenciation; Heat-shock protein; Heat-Shock Proteins - metabolism; Heparin - metabolism; Microbiology; Other techniques and industries; Protein Binding; RNA polymerase; Sigma factor; SpoOA; Spores, Bacterial; Sporulation
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(85)80373-2

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 σ 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.