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Related Concept Videos

Initiation of Translation02:33

Initiation of Translation

39.9K
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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Initiation of Translation02:33

Initiation of Translation

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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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Translation in Prokaryotes01:29

Translation in Prokaryotes

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Prokaryote translation is a complex, highly coordinated process that converts genetic information from mRNA into functional proteins. It involves three stages: initiation, elongation, and termination, each facilitated by specific molecular components.Initiation of TranslationThe process begins with the assembly of the ribosomal subunits and initiation factors on the mRNA. In bacteria, the 30S ribosomal subunit recognizes the Shine-Dalgarno sequence in the mRNA, a conserved region upstream of...
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Termination of Translation01:44

Termination of Translation

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The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
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Leaky Scanning02:28

Leaky Scanning

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During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
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Related Experiment Video

Updated: Mar 13, 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

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The Structures of eIF4E-eIF4G Complexes Reveal an Extended Interface to Regulate Translation Initiation.

Stefan Grüner1, Daniel Peter1, Ramona Weber1

  • 1Department of Biochemistry, Max Planck Institute for Developmental Biology, Spemannstrasse 35, 72076 Tübingen, Germany.

Molecular Cell
|November 5, 2016
PubMed
Summary

Eukaryotic initiation factor 4G (eIF4G) binds to eIF4E

Keywords:
4E-BPeIF4Fprotein-protein interactiontranslation initiationtranslational inhibitorstranslational regulation

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Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
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Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs
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Rapid In Vivo Fixation and Isolation of Translational Complexes from Eukaryotic Cells
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Rapid In Vivo Fixation and Isolation of Translational Complexes from Eukaryotic Cells

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Eukaryotic initiation factor 4G (eIF4G) is crucial for translation initiation.
  • eIF4G interacts with the cap-binding protein eIF4E, a key regulatory point.
  • 4E-binding proteins (4E-BPs) regulate this interaction and are drug targets.

Purpose of the Study:

  • To elucidate the binding mechanism of metazoan eIF4G auxiliary sequences to eIF4E.
  • To provide a molecular model of the eIF4E-eIF4G complex.
  • To inform the design of selective eIF4G inhibitors.

Main Methods:

  • X-ray crystallography
  • Analysis of human and Drosophila melanogaster eIF4E-eIF4G complexes

Main Results:

  • Crystal structures reveal eIF4G auxiliary sequences bind the lateral surface of eIF4E.
  • This binding mode is similar to that of 4E-BPs.
  • A detailed molecular model of the eIF4E-eIF4G complex was established.

Conclusions:

  • The study clarifies the competition between 4E-BPs and eIF4G for eIF4E binding.
  • The findings facilitate the rational design of inhibitors targeting eIF4G.
  • This could lead to therapeutic strategies for diseases with dysregulated translation.