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Related Concept Videos

Chromatin Structure Regulates pre-mRNA Processing02:41

Chromatin Structure Regulates pre-mRNA Processing

In eukaryotic cells, nascent mRNA transcripts need to undergo many post-transcriptional modifications to reach the cell cytoplasm and translate into functional proteins. For a long time, transcription and pre-mRNA processing were considered two independent events that occur sequentially in the cell. However, it has now been well established that transcription and pre-mRNA processing are two simultaneous processes that are precisely regulated inside the cell.
The chromatin structure, especially...
Transcription Elongation Factors02:35

Transcription Elongation Factors

Transcription elongation is a dynamic process that alters depending upon the sequence heterogeneity of the DNA being transcribed. Hence, it is not surprising that the elongation complex's composition also varies along the way while transcribing a gene.
The transcription elongation is regulated via pausing of RNA polymerase on several occasions during transcription. In bacteria, these halts are necessary because the transcription of DNA into mRNA is coupled to the translation of that mRNA into a...
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
Initiation of Translation02:33

Initiation of Translation

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...
Improving Translational Accuracy02:07

Improving Translational Accuracy

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...
The Unfolded Protein Response01:37

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...

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Related Experiment Video

Updated: May 9, 2026

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
08:47

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells

Published on: May 1, 2020

Human eIF4E promotes mRNA restructuring by stimulating eIF4A helicase activity.

Kateryna Feoktistova1, Enkhee Tuvshintogs, Angelie Do

  • 1Department of Molecular and Cell Biology, College of Biological Sciences, University of California, Davis, CA 95616, USA.

Proceedings of the National Academy of Sciences of the United States of America
|August 1, 2013
PubMed
Summary
This summary is machine-generated.

Elevated eukaryotic initiation factor 4E (eIF4E) levels promote cancer by enhancing translation of key mRNAs. This study reveals eIF4E

Keywords:
ATPaseDEAD-boxprotein synthesis

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Xenopus laevis as a Model to Identify Translation Impairment
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Xenopus laevis as a Model to Identify Translation Impairment

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Analysis of Cap-binding Proteins in Human Cells Exposed to Physiological Oxygen Conditions
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Analysis of Cap-binding Proteins in Human Cells Exposed to Physiological Oxygen Conditions

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Related Experiment Videos

Last Updated: May 9, 2026

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
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Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells

Published on: May 1, 2020

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Xenopus laevis as a Model to Identify Translation Impairment

Published on: September 27, 2015

Analysis of Cap-binding Proteins in Human Cells Exposed to Physiological Oxygen Conditions
10:40

Analysis of Cap-binding Proteins in Human Cells Exposed to Physiological Oxygen Conditions

Published on: December 28, 2016

Area of Science:

  • Molecular Biology
  • Cancer Research
  • Biochemistry

Background:

  • Elevated eukaryotic initiation factor 4E (eIF4E) levels are common in human cancers.
  • eIF4E overexpression drives cellular transformation by boosting translation of proliferative and prosurvival mRNAs.
  • The mechanism by which eIF4E abundance enhances translation of mRNAs with structured 5'-UTRs is not fully understood based on cap-binding alone.

Purpose of the Study:

  • To investigate the non-canonical functions of eIF4E in translation initiation.
  • To elucidate the mechanism by which eIF4E promotes translation of structured mRNAs.
  • To determine the role of eIF4E's interaction with eIF4G in regulating eIF4A activity.

Main Methods:

  • Biochemical assays to measure helicase activity.
  • In vitro translation assays.
  • Analysis of protein-protein interactions between eIF4E, eIF4G, and eIF4A.

Main Results:

  • eIF4E possesses a novel function that strongly stimulates the helicase activity of eukaryotic initiation factor 4A (eIF4A).
  • This eIF4E-mediated stimulation of eIF4A helicase activity is independent of eIF4E's cap-binding function.
  • The eIF4E-binding site on eIF4G acts as an autoinhibitory domain, which eIF4E binding relieves to enhance eIF4A stimulation.

Conclusions:

  • eIF4E has a dual role in translation initiation: cap-binding and stimulation of eIF4A helicase activity.
  • The helicase-promoting activity of eIF4E selectively enhances translation of structured mRNAs, distinct from its cap-binding function.
  • A sustained interaction between eIF4E and eIF4G during scanning likely explains how eIF4E abundance promotes translation of proliferation and tumor-promoting mRNAs.