Lon Protease is Needed to Resume Growth of Escherichia coli rpoH Mutant Following Gamma Radiation
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Heat shock proteins (HSPs) such as chaperones and proteases are upregulated toensure correct protein folding and to prevent the formation of toxic protein aggregates inresponse to heat shock or other insults that increase cellular protein misfolding. In Escherichiacoli, which has been used as a model organism in research in microbial genetics and physiology,HSPs are induced by temperature upshift from 30℃ to 42℃, and their induction is regulated bythe alternative sigma factor, σ32, encoded by the rpoH gene. The observation that post-irradiationincubation of E. coli at temperatures higher than 37°C resulted in increased survival rates hasled to the proposal that HSPs are required to survive stress from ionizing radiation. We haveinvestigated this hypothesis by examining the effects of rpoH mutation on cell survival and postirradiationrecovery. The wild-type E. coli strain (WT) exposed to gamma radiation (γ-radiation)exhibited a clear decrease in survival relative to non-irradiated counterparts, but there was nosignificant difference in the survival outcomes between WT and an rpoH mutant strain (ΔrpoH). When cells irradiated with doses of 1, 2, and 3 kGy were re-inoculated into fresh media, the lagphase of ΔrpoH became longer than that of WT in a dose-dependent manner. Expression of theheat shock protease Lon could partially restore the growth defect observed in irradiated ΔrpoH. These findings suggest that Lon may play a role in the post-irradiation recovery period bydegrading its primary substrate SulA, which inhibits cell division.
Abstract
Heat shock proteins (HSPs) such as chaperones and proteases are upregulated toensure correct protein folding and to prevent the formation of toxic protein aggregates inresponse to heat shock or other insults that increase cellular protein misfolding. In Escherichiacoli, which has been used as a model organism in research in microbial genetics and physiology,HSPs are induced by temperature upshift from 30℃ to 42℃, and their induction is regulated bythe alternative sigma factor, σ32, encoded by the rpoH gene. The observation that post-irradiationincubation of E. coli at temperatures higher than 37°C resulted in increased survival rates hasled to the proposal that HSPs are required to survive stress from ionizing radiation. We haveinvestigated this hypothesis by examining the effects of rpoH mutation on cell survival and postirradiationrecovery. The wild-type E. coli strain (WT) exposed to gamma radiation (γ-radiation)exhibited a clear decrease in survival relative to non-irradiated counterparts, but there was nosignificant difference in the survival outcomes between WT and an rpoH mutant strain (ΔrpoH). When cells irradiated with doses of 1, 2, and 3 kGy were re-inoculated into fresh media, the lagphase of ΔrpoH became longer than that of WT in a dose-dependent manner. Expression of theheat shock protease Lon could partially restore the growth defect observed in irradiated ΔrpoH. These findings suggest that Lon may play a role in the post-irradiation recovery period bydegrading its primary substrate SulA, which inhibits cell division.
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