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

[Oxytetracycline binding to E. coli ribosomes]

S A Strel'tsov, M K Kukhanova, G V Gurskiĭ

    Molekuliarnaia Biologiia
    |November 1, 1975
    PubMed
    Summary
    This summary is machine-generated.

    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

    Data on synthesis of methylene bisphosphonates and screening of their inhibitory activity towards HIV reverse transcriptase.

    Data in brief·2016
    Same author

    Methylene bisphosphonates as the inhibitors of HIV RT phosphorolytic activity.

    Biochimie·2016
    Same author

    Study of Antiherpetic Efficiency of Phosphite of Acycloguanosine Ableto Over come the Barrier of Resistance to Acyclovir.

    Acta naturae·2016
    Same author

    [Research of suppression of the herpes simplex virus reproduction with drug resistance by combination phosphite of acycloguanosine with some antiherpetic drugs].

    Voprosy virusologii·2015
    Same author

    [2'fluoro derivatives of nucleosides as substrates of viral replicative nucleotide polymerases].

    Molekuliarnaia biologiia·2015
    Same author

    Human herpes simplex virus: life cycle and development of inhibitors.

    Biochemistry. Biokhimiia·2015

    Oxytetracycline binds to E. coli ribosomes at one strong and many weak sites, forming magnesium chelates. This binding inhibits protein synthesis, likely through an allosteric mechanism.

    Area of Science:

    • Molecular Biology
    • Biochemistry
    • Microbiology

    Background:

    • Oxytetracycline is an antibiotic that inhibits bacterial protein synthesis.
    • Ribosomes are the cellular machinery responsible for protein synthesis.

    Purpose of the Study:

    • To investigate the binding mechanism of oxytetracycline to Escherichia coli ribosomes.
    • To elucidate the role of magnesium ions in this interaction.
    • To understand how oxytetracycline binding affects protein synthesis.

    Main Methods:

    • Equilibrium dialysis was used to study oxytetracycline-ribosome binding.
    • Analysis of magnesium chelate formation was performed.
    • The effect of aminoacyl-tRNA, poly(U), and chloramphenicol on binding was assessed.

    Related Experiment Videos

    Main Results:

    • Two classes of binding sites for oxytetracycline on ribosomes were identified: one strong and approximately 500 weak sites.
    • Oxytetracycline binds to ribosomes as magnesium chelates, with two types of chelates forming at different Mg2+ concentrations.
    • Strong oxytetracycline binding inhibits the association of aminoacyl-tRNA with ribosomes in a template-dependent manner.

    Conclusions:

    • Oxytetracycline exhibits specific binding to E. coli ribosomes, involving magnesium chelation.
    • The inhibition of protein synthesis by oxytetracycline appears to be mediated by an allosteric mechanism.
    • Further research is warranted to fully understand the allosteric regulation of protein synthesis by oxytetracycline.