STRESS-RESPONSE OF ESCHERICHIA-COLI TO ELEVATED HYDROSTATIC-PRESSURE

The response of exponentially growing cultures of Escherichia coli to abrupt shifts in hydrostatic pressure was studied. A pressure upshift to 546 atm (55,304 kPa) of hydrostatic pressure profoundly perturbed c ell division, nucleoid structure, and the total rate of protein synthe sis. The number of polypeptides synthesized at increased pressure was greatly reduced, and many proteins exhibited elevated rates of synthes is relative to total protein synthesis. We designated the latter prote ins pressure-induced proteins (PIPs). The PIP response was transient, with the largest induction occurring approximately 60 to 90 min postsh ift. Fifty-five PIPs were identified. Many of these proteins are also induced by heat shock or cold shock. The PIP demonstrating the greates t pressure induction was a basic protein of 15.6 kDa. High pressure in hibits growth but does not inhibit the synthesis of stringently contro lled proteins. Cold shock is the only additional signal which has been found to elicit this type of response. These data indicate that eleva ted pressure induces a unique stress response in E. coli, the further characterization of which could be useful in delineating its inhibitor y nature.