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Related Experiment Videos

Functional interactions between yeast translation eukaryotic elongation factor (eEF) 1A and eEF3.

Monika Anand1, Kalpana Chakraburtty, Matthew J Marton

  • 1Department of Molecular Genetics, Microbiology & Immunology, University of Medicine and Dentistry of New Jersey Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA.

The Journal of Biological Chemistry
|December 21, 2002
PubMed
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Eukaryotic elongation factor 3 (eEF3) is crucial for fungal protein synthesis, interacting with eEF1A to ensure translation accuracy. Disrupting this interaction impairs protein production and increases drug sensitivity.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Mycology

Background:

  • Fungal translation elongation differs from other eukaryotes due to reliance on eukaryotic elongation factor 3 (eEF3).
  • eEF3 is essential for fungal cell viability and plays a key role in the translation elongation cycle.
  • Models suggest eEF3 facilitates the removal of deacylated tRNA from the ribosomal exit site, a process linked to eEF1A function.

Purpose of the Study:

  • To investigate the functional relationship between eEF3 and eEF1A in fungal protein synthesis.
  • To characterize a novel temperature-sensitive allele of the YEF3 gene encoding eEF3.
  • To elucidate the molecular mechanisms underlying eEF3's role in translation elongation.

Main Methods:

  • Generation and characterization of a temperature-sensitive YEF3 allele (F650S).

Related Experiment Videos

  • Assays to measure ribosome-dependent and intrinsic ATPase activities of eEF3.
  • In vivo studies assessing protein synthesis rates, polyribosome run-off, and drug sensitivity.
  • Analysis of interactions between eEF3 and eEF1A, including binding affinities.

    • Main Results:

    • The F650S mutation in eEF3 impairs its ATPase activity and reduces binding to eEF1A.
    • In vivo, the F650S mutation leads to decreased protein synthesis, slower polyribosome run-off, and increased sensitivity to aminoglycosidic drugs.
    • Reciprocal experiments showed that excess eEF3 exacerbates the effects of an eEF1A mutation (E122K), indicating a critical interaction.
    • Mutant eEF1A (E122K) also exhibited reduced binding to eEF3.

    Conclusions:

    • Optimal in vivo interaction between eEF3 and eEF1A is essential for efficient and accurate fungal protein synthesis.
    • The study provides mechanistic insights into eEF3 function in translation elongation and its interplay with eEF1A.
    • Targeting the eEF3-eEF1A interaction could be a strategy for developing novel antifungal agents.