Disassembly of the coliphage lambda replication complex due to heat shock induction of the groE operon

Virology
A WegrzynK Taylor

Abstract

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.

Citations

Dec 18, 2008·Pakistan Journal of Biological Sciences : PJBS·M AhmadiH Dastmalchi Sale
Aug 26, 1998·Proceedings of the National Academy of Sciences of the United States of America·J ChatellierA R Fersht
May 9, 2006·Journal of Industrial Microbiology & Biotechnology·Sarah W Harcum, Fu'ad T Haddadin
Jun 22, 2002·Microbial Cell Factories·Grzegorz Wegrzyn, Alicja Wegrzyn
Mar 3, 2005·Biotechnology and Bioengineering·Fu'ad T Haddadin, Sarah W Harcum
Apr 28, 2007·Microbiology·Magdalena NarajczykGrzegorz Węgrzyn

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