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

Transfer RNA structure and coding specificity. II. A D-arm tertiary interaction that restricts coding range.

D Smith1, M Yarus

  • 1Department of Molecular, Cellular and Developmental Biology, University of Colorado, Boulder 80309.

Journal of Molecular Biology
|April 5, 1989
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

King's College Hospital's A&E department.

BMJ (Clinical research ed.)·1992
Same author

Garage door injuries in children.

CMAJ : Canadian Medical Association journal = journal de l'Association medicale canadienne·1992
Same author

Microinvasive carcinoma of the cervix.

Cancer·1992
Same author

Environmental and familial contributions to insulin levels and change in insulin levels in middle-aged women.

JAMA·1992
Same author

Pulmonary surfactant secretion is regulated by the physical state of extracellular phosphatidylcholine.

The Journal of biological chemistry·1992
Same author

Correlating CBC profile and infectious outcome. A study of febrile infants evaluated for sepsis.

Clinical pediatrics·1992
Same journal

UPF3A and UPF3B shape the transcriptome cooperatively yet oppose cell function.

Journal of molecular biology·2026
Same journal

Antibody-secreting cells integrate efficient NMD with non‑canonical UPR signaling to maintain proteostasis and support massive immunoglobulin synthesis.

Journal of molecular biology·2026
Same journal

Small molecule stabilization of diverse amyloidogenic immunoglobulin light chains revealed by hydrogen-deuterium exchange mass spectrometry.

Journal of molecular biology·2026
Same journal

UPF1 at Work: Structural and Mechanistic Insights Into a Master Regulator of Nonsense-Mediated mRNA Decay.

Journal of molecular biology·2026
Same journal

Structural basis for the pro-amyloidogenic action and ligand binding of a novel W72R variant of human apolipoprotein A-I.

Journal of molecular biology·2026
Same journal

Cryo-EM Structure of the C. Elegans Septin Tetramer Reveals a Revised Architecture and Conserved Positional Orthology.

Journal of molecular biology·2026
See all related articles

A specific mutation in Escherichia coli tRNA Trp

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • Transfer RNA (tRNA) plays a crucial role in protein synthesis by decoding messenger RNA (mRNA) codons.
  • The D-arm of tRNA is known to influence tRNA structure and function.
  • Mutations in tRNA can alter its coding specificity and translational efficiency.

Purpose of the Study:

  • To investigate the structural basis for the kinetic effect of a D-arm mutation (G24 to A) on the coding specificity of Escherichia coli tRNA Trp.
  • To understand the role of specific base pairings and tRNA conformation in modulating translational kinetics and coding fidelity.

Main Methods:

  • Site-directed mutagenesis was used to create tRNA genes with alterations in the D-arm.
  • In vivo translational activities of mutant tRNAs were determined.

Related Experiment Videos

  • tRNA crystal structures were inspected to identify potential tertiary interactions.
  • Mutations at position 9 were introduced to assess their impact on D-arm mutant phenotypes.

    • Main Results:

    • A hydrogen-bond donor at position 24 in the D-helix is essential for expanded tRNA wobble coding specificity.
    • A novel tertiary interaction between base 24 and base 9 was identified.
    • The phenotypes of D-arm mutants (positions 11-24) depend on the identity of base 9.
    • Mutations affect tRNA interactions with the ribosome and aminoacyl-tRNA synthetase, altering translational kinetics.

    Conclusions:

    • The conformation or dynamics of the central tRNA region modulate interaction kinetics with the ribosomal coding site.
    • Specific tertiary interactions, including the 9-23 and putative 9-24 pairings, fine-tune these kinetics to regulate coding specificity.
    • Understanding these mechanisms is key to comprehending translational fidelity and the impact of tRNA modifications.