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

The binding sites for tRNA on eukaryotic ribosomes.

D P Leader, G C Machray

    Nucleic Acids Research
    |July 1, 1975
    PubMed
    Summary

    Phenylalanyl-tRNA (phe-tRNA) non-enzymic binding to eukaryotic ribosomes is magnesium-dependent. At high magnesium concentrations, phe-tRNA binds to both A and P sites, unlike at low concentrations.

    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

    Exploiting plant somatic radiation hybrids for physical mapping of expressed sequence tags.

    TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik·2003
    Same author

    Tuberization in potato involves a switch from apoplastic to symplastic phloem unloading.

    The Plant cell·2001
    Same author

    Identification of sites phosphorylated by the vaccinia virus B1R kinase in viral protein H5R.

    BMC biochemistry·2000
    Same author

    Differential expression of invertase genes in internal and external phloem tissues of potato (Solanum tuberosum L.).

    Journal of experimental botany·2000
    Same author

    Requirements for mini-exon inclusion in potato invertase mRNAs provides evidence for exon-scanning interactions in plants.

    RNA (New York, N.Y.)·2000
    Same author

    Expression of tandem invertase genes associated with sexual and vegetative growth cycles in potato.

    Plant molecular biology·2000

    Area of Science:

    • Molecular Biology
    • Ribosome Function
    • Protein Synthesis

    Background:

    • Non-enzymic binding of aminoacyl-tRNA to ribosomes is a crucial step in protein synthesis.
    • Understanding the distinct binding sites (A-site and P-site) on eukaryotic ribosomes is essential for elucidating translation mechanisms.
    • Differences in ribosome structure and function between eukaryotes and prokaryotes impact tRNA binding.

    Purpose of the Study:

    • To investigate the non-enzymic binding of phenylalanyl-tRNA (phe-tRNA) to rat liver ribosomes.
    • To determine the influence of magnesium ion concentration on phe-tRNA binding sites.
    • To compare the non-enzymic binding characteristics of eukaryotic ribosomes with prokaryotic ribosomes.

    Main Methods:

    • Utilized deacylated tRNA to inhibit binding to the P-site.
    • Employed puromycin to inhibit binding to the A-site.
    • Studied the effects of low (10mM) and high (40mM) magnesium ion concentrations.
    • Investigated ribosome-edine interactions.

    Main Results:

    • At low magnesium concentrations (10mM), phe-tRNA exclusively binds to the A-site of 80S ribosomes.
    • At high magnesium concentrations (40mM), phe-tRNA binds to both the A-site and P-site of 80S ribosomes.
    • Eukaryotic ribosomes exhibit juxtaposed A-sites (60S subunit) and initiation sites (40S subunit) during non-enzymic phe-tRNA binding, differing from prokaryotic ribosomes.

    Conclusions:

    • Magnesium ion concentration dictates the P-site occupancy of phe-tRNA during non-enzymic binding to eukaryotic ribosomes.
    • The juxtaposed arrangement of ribosomal sites in eukaryotes may explain observed differences in diphenylalanyl-tRNA and phenylalanyl-puromycin formation compared to prokaryotes.

    Related Experiment Videos