Disassembly of the coliphage lambda replication complex due to heat shock induction of the groE operon.
We have found previously that, in contrast to the free O initiator protein of lambda phage or plasmid rapidly degraded by the Escherichia coli ClpP/ClpX protease, the lambda O present in the replication complex (RC) is protected from proteolysis. In amino acid-starved E. coli relA cells, a temperature shift from 30 to 43 degrees did not affect RC integrity, as judged from the unchanged level of stable lambda O observed; however, the same temperature shift in a complete medium resulted in the decay of this lambda O fraction, which suggested disassembly of the RC. Examination of this phenomenon revealed that for lambda RC disassembly, heat shock induction of the groE operon, coding for molecular chaperones of the Hsp60 class, is indispensable. Heat shock induction of the groE operon present on a multicopy plasmid inhibited the growth of infecting phage.
Wegrzyn
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A
Laboratory of Molecular Biology, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Gdansk.
Wegrzyn
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G
Taylor
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K
D001426:Bacterial Proteins / Q000502:physiology*; D010582:Bacteriophage lambda / Q000254:growth & development*; D018833:Chaperonins; D004261:DNA Replication; D004926:Escherichia coli / Q000235:genetics; D029968:Escherichia coli Proteins; D015967:Gene Expression Regulation, Viral; D006360:Heat-Shock Proteins / Q000502:physiology*; D006358:Hot Temperature; D018832:Molecular Chaperones / Q000502:physiology; D009875:Operator Regions, Genetic; D014779:Virus Replication
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C028715:GroE protein, E coli; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D018833:Chaperonins