Protein aggregation and inclusion body formation in Escherichia coli rpoH mutant defective in heat shock protein induction

• Published in: FEBS letters Vol. 291; no. 2; pp. 222 - 224
• Main Authors: Gragerov, A.I., Martin, E.S., Krupenko, M.A., Kashlev, M.V., Nikiforov, V.G.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 21-10-1991; Elsevier
• Subjects: aggregation; Analytical, structural and metabolic biochemistry; Biological and medical sciences; Chaperone; characterization; deficiency; Escherichia coli; Escherichia coli - genetics; Escherichia coli - physiology; Escherichia coli - ultrastructure; Fundamental and applied biological sciences. Psychology; Genes, Bacterial; Heat shock protein; heat shock proteins; Heat-Shock Proteins - biosynthesis; Heat-Shock Proteins - chemistry; Heat-Shock Proteins - genetics; inclusion bodies; Inclusion body; Mutation; Protein Conformation; Protein folding; Proteins; rpoH mutant; Inclusion body; rpoH mutant; Protein folding; Chaperone; Heat shock protein; Aggregation; Proteins; Induction; Escherichia coli; Bacteria; Mutation; Enterobacteriaceae
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(91)81289-K

Mutations in the
rpoH gene, encoding σ
32, an alternative factor required for transcription of the heat shock genes, result in the extensive aggregation of virtually all cellular proteins and formation of inclusion bodies both under stress and non-stress conditions. Inhibitors of protein synthesis suppress this aggregation, suggesting that newly synthesized proteins preferentially aggregate in
rpoH mutants. These data suggest that the heat shock proteins are involved in acquisition of the soluble state (i.e. correct conformation) of the bulk of intracellular proteins after their translation.