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Related Concept Videos

Initiation of Translation02:33

Initiation of Translation

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Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...
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Replication in Eukaryotes02:31

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The Eukaryotic Promoter Region02:40

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The eukaryotic promoter region is a segment of DNA located upstream of a gene. It contains an RNA polymerase binding site, a transcription start site, and several cis-regulatory sequences.  The proximal promoter region is located in the vicinity of the gene and has cis-regulatory sequences and the core promoter. The core promoter is the binding site for RNA polymerase and is usually located between -35 and +35 nucleotides from the transcription start site. The distal promoter regions are...
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Eukaryotic RNA Polymerases00:58

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RNA Polymerase (RNAP) is conserved in all animals, with bacterial, archaeal, and eukaryotic RNAPs sharing significant sequence, structural, and functional similarities. Among the three eukaryotic RNAPs, RNA Polymerase II is most similar to bacterial RNAP in terms of both structural organization and folding topologies of the enzyme subunits. However, these similarities are not reflected in their mechanism of action.
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Improving Translational Accuracy02:07

Improving Translational Accuracy

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Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
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Updated: Jan 30, 2026

Analysis of Translation Initiation During Stress Conditions by Polysome Profiling
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Biochemical and Structural Insights into the Eukaryotic Translation Initiation Factor eIF4E.

Laurent Volpon1, Michael J Osborne1, Katherine L B Borden1

  • 1Institute for Research in Immunology and Cancer (IRIC), Department of Pathology and Cell Biology, Universite de Montreal, Pavillion Marcelle-Coutu, Chemin Polytechnique, Montreal, Quebec, Canada.

Current Protein & Peptide Science
|January 15, 2019
PubMed
Summary

The eukaryotic translation initiation factor eIF4E regulates protein production post-transcriptionally. Targeting eIF4E shows promise in cancer treatment by modulating RNA metabolism and protein levels.

Keywords:
RNA stability; clinical trialseIF4EeIF4E regulatorsmRNA exportribavirintranslation initiation factor.

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Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
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Area of Science:

  • Cell Biology
  • Cancer Biology
  • Molecular Biology

Background:

  • The proteome can differ from the transcriptome due to post-transcriptional regulation.
  • The eukaryotic translation initiation factor eIF4E (eIF4E) is crucial in post-transcriptional control and is elevated in many cancers.

Purpose of the Study:

  • To review the functions of eIF4E in RNA metabolism.
  • To explore the biochemical and structural regulation of eIF4E.
  • To discuss the clinical relevance of targeting eIF4E.

Main Methods:

  • Literature review of eIF4E functions in RNA metabolism (export, translation, stability).
  • Analysis of biochemical and structural data on eIF4E regulation.
  • Overview of clinical trials targeting eIF4E.

Main Results:

  • eIF4E regulates nuclear-cytoplasmic RNA export, translation, and RNA stability/sequestration.
  • Regulation occurs through traditional m7G cap interactions, non-traditional RNA interactions, and cap-independent activities.
  • Diverse structural mechanisms regulate eIF4E, involving proteins beyond traditional eIF4E-binding proteins.

Conclusions:

  • eIF4E plays a significant role in post-transcriptional gene expression and cancer.
  • Understanding eIF4E's diverse regulatory mechanisms is key.
  • Targeting eIF4E presents a viable therapeutic strategy for cancer.