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Response of Escherichia coli cell membranes to induction of λc1857 prophage by heat shock

Heat shock induces protein aggregation in Escherichia coli and E. coli (λc1857). The aggregates (S fraction) appear 15 min post‐induction and are separable from membranes by sucrose density‐gradient centrifugation. The S fraction quickly disappears in wild type strains but persists in rpoH mutant with concomitant quick inner membrane destruction. We propose that: (1) the disappearance of the S fraction reflects a rpoH‐dependent processing, (2) the membrane destruction explains the lethality of the rpoH mutation at elevated temperatures; and (3) the protection of the inner membrane integrity is an important physiological function of the heat‐shock response. We assume that the S fraction of aggregated proteins represents the signal inducing the heat‐shock response.