Pope D H, Connors N T, Landau J V
J Bacteriol. 1975 Mar;121(3):753-8. doi: 10.1128/jb.121.3.753-758.1975.
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.
在转录起始被利福平阻断的活跃生长细胞中，研究了增加流体静压力时大肠杆菌多核糖体的稳定性。在这些细胞中，可以观察到[3-H]尿苷掺入信使核糖核酸以及随后核糖核酸酶对信使（进而对多核糖体）的降解。有证据表明，核糖核酸酶的活性不受680个大气压压力的影响，蛋白质合成在680个大气压时完全被抑制，但压力释放后立即以1个大气压时的速率恢复，并且在680个大气压时多核糖体中的信使核糖核酸不会发生降解。讨论了压力、嘌呤霉素和氯霉素对多核糖体降解的影响。这些结果表明，与之前的一些报道相反，多核糖体可能在高压下得到稳定。因此，我们认为多核糖体不稳定性不是高压抑制蛋白质合成的一个因素。
