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

Major anticodon-binding region missing from an archaebacterial tRNA synthetase.

B A Steer1, P Schimmel

  • 1The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA.

The Journal of Biological Chemistry
|December 10, 1999
PubMed
Summary

The small Methanococcus jannaschii tyrosyl-tRNA synthetase enzyme lacks an anticodon-binding domain, suggesting anticodon interactions evolved later in tRNA synthetase development. This enzyme maintains minihelix specificity, crucial for early aminoacylation. Keywords: tyrosyl-tRNA synthetase, tRNA, anticodon, minihelix.

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

[Analysis of clinical pathway in changing and disabling neurological diseases].

Revue neurologique·2013
Same author

RNA scaffolds for minihelix-based aminoacyl transfer: design of "transpeptizymes".

Journal of biomolecular structure & dynamics·2012
Same author

A model of ischemic isolated acute liver failure in pigs: standardizing monitoring and treatment.

European surgical research. Europaische chirurgische Forschung. Recherches chirurgicales europeennes·2010
Same author

The novel fragment of tyrosyl tRNA synthetase, mini-TyrRS, is secreted to induce an angiogenic response in endothelial cells.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology·2008
Same author

Artificially ambiguous genetic code confers growth yield advantage.

Proceedings of the National Academy of Sciences of the United States of America·2004
Same author

Biologically active fragment of a human tRNA synthetase inhibits fluid shear stress-activated responses of endothelial cells.

Proceedings of the National Academy of Sciences of the United States of America·2003

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Transfer RNAs (tRNAs) and their synthetases are crucial for protein synthesis.
  • The structure of tRNA synthetases parallels tRNA structure, with ancient and recent domains.
  • Methanococcus jannaschii tyrosyl-tRNA synthetase (TyrRS) is unusually small.

Purpose of the Study:

  • To investigate the evolutionary implications of the small size of M. jannaschii TyrRS.
  • To understand the role of different domains in tRNA synthetase function and evolution.
  • To examine the substrate specificity and temperature activity of M. jannaschii TyrRS.

Main Methods:

  • Comparative structural analysis of M. jannaschii TyrRS and other synthetases.
  • Site-directed mutagenesis of the tRNA anticodon.

Related Experiment Videos

  • Enzymatic assays measuring aminoacylation efficiency across a temperature range.

    • Main Results:

    • M. jannaschii TyrRS lacks significant portions of the anticodon-binding domain found in larger synthetases.
    • Anticodon mutations had minimal impact on M. jannaschii TyrRS aminoacylation efficiency, unlike bacterial enzymes.
    • The enzyme retains a critical minihelix-binding peptide insertion and shows temperature-stable minihelix specificity.

    Conclusions:

    • The small size of M. jannaschii TyrRS is attributed to the reduction of its anticodon-binding domain.
    • This supports the hypothesis that anticodon interactions were a later evolutionary adaptation in synthetase-tRNA recognition.
    • The minihelix interaction remains a conserved, fundamental feature of tyrosyl-tRNA synthetase function.