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

Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by

Lars Fichtner1, Daniel Jablonowski, Angelika Schierhorn

  • 1Biologicum, Institut für Genetik, Martin-Luther-Universität Halle-Wittenberg, Weinbergweg 10, D-06120 Halle (Saale), Germany.

Molecular Microbiology
|August 28, 2003
PubMed
Summary

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

Evolutionary conservation of ubiquitin-like protein urmylation as revealed by URM1 gene shuffle from archaea to yeast.

Communications biology·2025
Same author

Autophosphorylation of conserved yeast and human casein kinase 1 isozymes regulates Elongator-dependent tRNA modifications.

Nucleic acids research·2025
Same author

tRNA binding to Kti12 is crucial for wobble uridine modification by Elongator.

Nucleic acids research·2025
Same author

Diphthamide formation in Arabidopsis requires DPH1-interacting DPH2 for light and oxidative stress resistance.

Plant physiology·2025
Same author

Diphthamide synthesis is linked to the eEF2-client chaperone machinery.

FEBS letters·2025
Same author

Cryo-EM structures of the human Elongator complex at work.

Nature communications·2024

The Elongator complex

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The Elongator complex in Saccharomyces cerevisiae is crucial for the toxin target (TOT) function.
  • This function is essential for Kluyveromyces lactis zymocin to induce cell cycle arrest.
  • Post-translational modification and proteolysis of Elongator subunit Tot1p (Elp1p) impact its TOT function.

Purpose of the Study:

  • To investigate the molecular mechanisms underlying the Elongator complex's toxin target (TOT) function.
  • To identify proteins interacting with the Elongator complex and their role in zymocin-induced cell cycle arrest.
  • To elucidate the role of nuclear import in Elongator's TOT function.

Main Methods:

  • TAP tagging to identify protein interactions.

Related Experiment Videos

  • Analysis of gene deletions affecting Elongator modification and function.
  • Localization studies using green fluorescent protein (GFP) fusions and nuclear localization sequences (NLS).

    • Main Results:

    • Loss of ubiquitin-related system (URM1-UBA4) and KTI11 leads to increased Tot1p modification/proteolysis and abrogates TOT function.
    • Kti11p interacts with Elongator and translational proteins, suggesting a role in toxin response.
    • Loss of YIL103w and DPH2 suppresses zymocin toxicity, indicating overlapping pathways mediated by Kti11p.
    • Unmodified Tot1p is found in a complex with RNA polymerase II (pol II) and nucleolin.
    • Elongator's nuclear import via NLS and karyopherin-dependent import is essential for its TOT function.

    Conclusions:

    • Post-translational modification and proteolysis of Elongator may regulate its association with pol II and cellular localization.
    • The Elongator complex's toxin target (TOT) function is dependent on its nuclear import pathway.
    • Kti11p acts as a scaffold, linking Elongator to translational machinery and potentially mediating overlapping toxin response pathways.