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Related Experiment Video

Updated: Jun 19, 2025

Electrophoretic Mobility Shift Assay EMSA for the Study of RNA-Protein Interactions: The IRE/IRP Example
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Functional Activity of Isoform 2 of Human eRF1.

Alexey Shuvalov1,2, Alexandr Klishin1, Nikita Biziaev1

  • 1Engelhardt Institute of Molecular Biology, The Russian Academy of Sciences, 119991 Moscow, Russia.

International Journal of Molecular Sciences
|July 27, 2024
PubMed
Summary

A newly discovered human eRF1 isoform 2 plays a role in regulating translation termination. This unstudied isoform interacts with ribosomal subunits but shows reduced activity, impacting stop codon readthrough and translation efficiency.

Keywords:
eRF1eRF3readthroughribosometranslation termination

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A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α
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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Eukaryotic release factor 1 (eRF1), encoded by ETF1, is crucial for recognizing stop codons and terminating translation.
  • Alternative splicing of ETF1 generates multiple transcripts, including two eRF1 isoforms: the canonical isoform 1 and a shorter, unstudied isoform 2.
  • Isoform 2 is 33 amino acids shorter than isoform 1 and its function remains largely unknown.

Purpose of the Study:

  • To investigate the function and characteristics of the unstudied human eRF1 isoform 2.
  • To determine the role of eRF1 isoform 2 in translation termination and its interaction with other translation factors.
  • To explore the potential regulatory functions of eRF1 isoform 2 in gene expression.

Main Methods:

  • Utilized a reconstituted mammalian in vitro translation system.
  • Analyzed interactions between eRF1 isoform 2 and ribosomal subunits/pre-termination complexes.
  • Assessed codon recognition, peptide release, GTPase activity stimulation, stop codon readthrough, and translation efficiency in cell-free systems.

Main Results:

  • eRF1 isoform 2 interacts with ribosomal subunits and pre-termination complexes but exhibits reduced codon recognition and peptide release activities.
  • eRF1 isoform 2 shows unipotency to UGA codons and interacts less effectively with eRF3a, poorly stimulating its GTPase activity.
  • eRF1 isoform 2 suppresses stop codon readthrough and decreases translation efficiency for long coding sequences.

Conclusions:

  • Human eRF1 isoform 2 is involved in translation, potentially regulating translation termination.
  • The GTS loop is important for eRF1's multipotency to all stop codons.
  • Helix α1 of the N-domain may be involved in conformational changes facilitating peptidyl-tRNA hydrolysis.