Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Enzymatic adaptation by bacteria under pressure

R E Marquis, D M Keller

    Journal of Bacteriology
    |May 1, 1975
    PubMed
    Summary
    This summary is machine-generated.

    Hydrostatic pressure impacts bacterial enzyme adaptation differently. Some processes are pressure-insensitive, while others, like lac operon derepression, are barosensitive, affecting bacterial growth and survival under pressure.

    Related Concept Videos

    You might also read

    Related Articles

    Articles linked to this work by shared authors, journal, and citation graph.

    Sort by
    Same author

    Modification of χ_{c1}(3872) and ψ(2S) Production in pPb Collisions at sqrt[s_{NN}]=8.16  TeV.

    Physical review letters·2024
    Same author

    Amplitude Analysis of the B^{0}→K^{*0}μ^{+}μ^{-} Decay.

    Physical review letters·2024
    Same author

    Fraction of χ_{c} Decays in Prompt J/ψ Production Measured in pPb Collisions at sqrt[s_{NN}]=8.16  TeV.

    Physical review letters·2024
    Same author

    Enhanced Production of Λ_{b}^{0} Baryons in High-Multiplicity pp Collisions at sqrt[s]=13  TeV.

    Physical review letters·2024
    Same author

    Observation of Cabibbo-Suppressed Two-Body Hadronic Decays and Precision Mass Measurement of the Ω_{c}^{0} Baryon.

    Physical review letters·2024
    Same author

    Improved Measurement of CP Violation Parameters in B_{s}^{0}→J/ψK^{+}K^{-} Decays in the Vicinity of the ϕ(1020) Resonance.

    Physical review letters·2024

    Area of Science:

    • Microbiology
    • Biochemistry
    • Environmental Science

    Background:

    • Bacteria exhibit varying degrees of tolerance to hydrostatic pressure.
    • Enzymic adaptation is crucial for bacterial survival and function in different environments.
    • Understanding pressure effects on microbial processes informs biotechnology and deep-sea exploration.

    Purpose of the Study:

    • To investigate the impact of hydrostatic pressure on bacterial enzymic adaptation.
    • To differentiate between pressure-insensitive and pressure-sensitive adaptive mechanisms.
    • To elucidate the molecular mechanisms underlying pressure-induced inhibition of enzyme synthesis.

    Main Methods:

    • Studied moderately barotolerant bacteria, including Escherichia coli and Bacillus licheniformis.

    Related Experiment Videos

  • Assessed enzyme adaptation to substrates like arabinose and lactose under pressures up to 500 atm.
  • Investigated the lac operon derepression and penicillinase synthesis under varying pressure conditions.
  • Analyzed the effect of cyclic adenosine 5'-monophosphate and inducer concentrations on pressure sensitivity.
  • Main Results:

    • Some adaptive processes (e.g., arabinose catabolism in E. coli) were pressure-insensitive.
    • Other processes (e.g., lac operon derepression, penicillinase induction) were barosensitive, with pressures of 300-400 atm reducing enzyme synthesis rates.
    • Pressure inhibited enzyme synthesis but not substrate uptake (beta-galactosides).
    • Apparent volume changes suggested pressure affects inducer binding and complex formation.

    Conclusions:

    • Bacterial adaptation to hydrostatic pressure is complex, with distinct pressure sensitivities for different enzymatic systems.
    • Pressure-sensitive mechanisms, like lac operon regulation, can compromise bacterial survival and growth under high pressure.
    • The findings provide insights into the biophysical constraints on microbial life in high-pressure environments.