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Protein aggregation and inclusion body formation in Escherichia coli rpoH mutant defective in heat shock protein induction
Author(s) -
Gragerov A.I.,
Martin E.S.,
Krupenko M.A.,
Kashlev M.V.,
Nikiforov V.G.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81289-k
Subject(s) - escherichia coli , heat shock protein , mutant , chemistry , protein aggregation , heat shock , microbiology and biotechnology , biochemistry , biology , gene
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.