Low temperature‐induced systems failure in Escherichia coli: Insights from rescue by cold‐adapted chaperones

• Published in: PROTEOMICS
• Main Authors: Strocchi, Massimo, Ferrer, Manuel, Timmis, Kenneth N., Golyshin, Peter N.
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 2006
• Subjects: Antarc*; Antarctica
• Online Access: http://dx.doi.org/10.1002/pmic.200500031; http://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fpmic.200500031; https://onlinelibrary.wiley.com/doi/full/10.1002/pmic.200500031

Abstract The growth of Escherichia coli cells is impaired at temperatures below 21°C and stops at 7.5°C; however, growth of a transgenic strain producing the cold‐adapted chaperones Cpn60 and Cpn10 from the psychrophilic bacterium Oleispira antarctica is good at low temperatures. The E. coli cpn + transgene offers a novel opportunity for examining the essential protein for cell viability at low temperatures. By screening a large‐scale protein map (proteome) of cells of K‐12 and its Cpn + transgene incubated at 4°C, we identified 22 housekeeping proteins involved in systems failure of E. coli when confronted with low temperature. Through co‐immunoprecipitation of Cpn60, Northern blot, and in vitro refolding, we systematically identified that protein–chaperone interactions are key determinants of their protein functions at low temperatures. Furthermore, chromosomal gene deletion experiments suggest that the mechanism of cold‐induced systems failure in E. coli is cold‐induced inactivation of the GroELS chaperonins and the resulting failure to refold cold‐inactivated Dps, ClpB, DnaK and RpsB proteins. These findings: (1) indicate the potential importance of chaperones in cold sensitivity, cold adaptation and cold tolerance in cellular systems, and (2) suggest the identity of a few key cold‐sensitive chaperone‐interacting proteins that get inactivated and ultimately cause systems failure in E. coli cells at low temperatures.