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Role of molecular chaperones in cold adaptation of bacteria

The role of HSPs in cold adaptation of bacteria is beginning to be understood. It was shown a couple of years ago that rate of survival of a strain of Escherichia coli after incubation at -80oC for 24 hours could be significantly improved by warming the solution at 42 o C for 30 minutes before cold storage. The induction of the heat shock proteins (Dna K/Dna J) in the heat treated sample was also demonstrated (Chow and Tung 1998). The Clp B protein, which is essential for thermotolerance in Cyanobacteria and Eukaryotes, was found to be induced by moderate chilling in the cyanobacterial strain Synechococcus PCC 7942. Following a shift from 37oC to 25oC, growth and photosynthesis were more adversely affected in a mutant having deletion in the clp B gene, compared to the wild type Synechococcus PCC 7942 (Porankiewicz and Clarke 1997). The role of the Htp G protein (a prokaryotic homolog of the heat shock protein Hsp 90) in both thermal adaptation and cold acclimation of the same organism was also reported some time back (Hossain and Nakamoto 2002).