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J Bacteriol. 1972 December; 112(3): 1222-1227
Copyright © 1972 American Society for Microbiology. All Rights Reserved.

Inhibition of Cell-Free Protein Synthesis by Hydrostatic Pressure1

J. R. Schwarz and J. V. Landau

a Department of Biology, Rensselaer Polytechnic Institute, Troy, New York 12181

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 ({Delta}V*) 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 ({Delta}V*) 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.

FOOTNOTES

1 This paper is taken in part from a thesis that was submitted by J. R. S. in partial fulfillment of the requirements for the degree of Doctor of Philosophy in the Department of Biology, Rensselaer Polytechnic Institute.

J Bacteriol. 1972 December; 112(3): 1222-1227
Copyright © 1972 American Society for Microbiology. All Rights Reserved.





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