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Related Experiment Videos

Hydrostatic pressure effects on protein synthesis.

C E Hildebrand, E C Pollard

    Biophysical Journal
    |October 1, 1972
    PubMed
    Summary
    This summary is machine-generated.

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    High hydrostatic pressure initially boosts cell-free protein synthesis but then inhibits it, affecting translation fidelity and aminoacyl-tRNA activation. Ribosomes appear to be the primary pressure-sensitive component.

    Area of Science:

    • Molecular Biology
    • Biophysics

    Background:

    • Cell-free protein synthesis is crucial for understanding translation.
    • High hydrostatic pressure (HHP) can alter biological processes.

    Purpose of the Study:

    • To investigate the impact of HHP on cell-free protein synthesis.
    • To identify pressure-sensitive steps and components in the protein synthesis machinery.

    Main Methods:

    • Examined polyuridylic acid (poly U)-directed polyphenylalanine synthesis under varying hydrostatic pressures.
    • Assessed misreading of the genetic code, transfer RNA (tRNA) aminoacylation, and complex stability.

    Main Results:

    • HHP initially increased synthesis rate but then caused significant inhibition (>95% at 640 atm).

    Related Experiment Videos

  • Pressure-induced inhibition was dependent on magnesium salt concentration.
  • Misreading of the poly U message initially decreased then increased with pressure.
  • Enzymatic tRNA activation and non-enzymatic attachment/stability of phenylalanyl-tRNA (phe-tRNA) to ribosomes were reduced by HHP.

    • Conclusions:

    • The ribosome is identified as the major pressure-sensitive element in protein synthesis.
    • HHP affects multiple stages of translation, including initiation, elongation, and fidelity.