Stability of Escherichia coli polysomes at high hydrostatic pressure.

The stability of Escherichia coli polysomes at increased hydrostatic pressure was investigated in actively growing cells, in which the initiation of transcription was blocked by rifampin. In these cells, [3-H]uridine incorporation into messenger ribonucleic acid and the subsequent degradation of the message (and therefore of polysomes) by ribonuclease could be observed. Evidence is presented that the activity of the RNases is unaffected by a pressure of 680 atm, that protein synthesis is completely inhibited at 680 atm but immediately resumes at the 1 atm rate on release of pressure, and that no degradation of messenger ribonucleic acid in polysomes occurs at 680 atm. The effects of pressure; puromycin, and chloramphenicol on polysomal degradation are discussed. These results indicate that, contrary to some previous reports, polysomes are probably stabilized by high pressures. Therefore, we consider that polysomal instability is not a factor in the inhibition of protein synthesis by high pressures.