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. 1972 Dec;112(3):1222–1227. doi: 10.1128/jb.112.3.1222-1227.1972

Inhibition of Cell-Free Protein Synthesis by Hydrostatic Pressure1

J R Schwarz a, J V Landau a
PMCID: PMC251552  PMID: 4565535

Abstract

Pressure inhibition of cell-free polypeptide synthesis is manifested in the same manner as that observed in the intact cell: (i) starting at approximately 200 atm, there is a progressive inhibition with increasing pressures; (ii) there is complete inhibition at 680 atm; (iii) incorporation into polypeptide is instantaneously reversible after pressure release and proceeds at a rate parallel to an atmospheric control; and (iv) the volume change of activation (ΔV*) is 100 cm3/mole. Peptide bond formation per se can occur at a pressure level which is totally inhibitory to polypeptide synthesis. The one investigated step in translation that is inhibited in an identical manner is the binding of aminoacyl-transfer ribonucleic acid (AA-tRNA) to the ribosome-messenger RNA (mRNA) complex. The volume change of activation (ΔV*) calculated for the binding reaction is also 100 cm3/mole. Thus, the inability of AA-tRNA to bind to ribosomes and mRNA under pressure, possibly in conjunction with translocation, appears to be responsible for the observed inhibition of the translational mechanism.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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