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Related Concept Videos

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...
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...
Leaky Scanning02:28

Leaky Scanning

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 stands for...
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...
Nonsense-mediated mRNA Decay02:27

Nonsense-mediated mRNA Decay

The Upf proteins that carry out nonsense-mediated decay (NMD) are found in all eukaryotic organisms, including humans. Each protein has an individual role, but they need to work in collaboration. Upf1 is an ATP-dependent RNA helicase that unwinds the RNA helix. Because Upf1 can unwind any RNA, Upf2 and Upf3 are required to help Upf1 discriminate between nonsense and normal mRNAs.
Usually, Upf3 binds to an Exon Junction Complex (EJC) at mRNA splice sites. If a ribosome fully translates the mRNA,...
Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
Ribosome biogenesis begins with the synthesis of 5S and 45S pre-rRNAs by distinct RNA polymerases. The primary transcripts are extensively processed and modified before they are bound and folded by ribosomal proteins and assembly factors,...

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Related Experiment Video

Updated: May 28, 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

Structural basis for nematode eIF4E binding an m(2,2,7)G-Cap and its implications for translation initiation.

Weizhi Liu1, Marzena Jankowska-Anyszka, Karolina Piecyk

  • 1Department of Biochemistry and Molecular Genetics, University of Colorado School of Medicine, Aurora, CO 80045, USA.

Nucleic Acids Research
|October 4, 2011
PubMed
Summary

The study reveals how nematode eIF4E binds to two different mRNA caps, m⁷G-cap and m(2,2,7)G-cap, impacting translation initiation. Interactions with the spliced leader RNA influence this process, affecting 5'-UTR roles in translation.

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Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs
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Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs

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Related Experiment Videos

Last Updated: May 28, 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

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

Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs
10:37

Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs

Published on: May 10, 2018

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Metazoan spliced leader (SL) trans-splicing produces mRNAs with a unique m(2,2,7)G-cap.
  • The mechanism of eukaryotic initiation factor 4E (eIF4E) binding to the m(2,2,7)G-cap is not well understood.
  • Understanding cap-binding is crucial for deciphering mRNA translation regulation.

Purpose of the Study:

  • To elucidate the structural basis of eIF4E binding to the m(2,2,7)G-cap.
  • To compare the binding of m(2,2,7)G-cap and m⁷G-cap by eIF4E.
  • To investigate the role of the spliced leader (SL) RNA in eIF4E interactions and translation initiation.

Main Methods:

  • X-ray crystallography to determine the structure of Ascaris suum eIF4E bound to the m(2,2,7)G-cap.
  • Comparison with the known structure of eIF4E bound to m⁷G-cap.
  • Nuclear Magnetic Resonance (NMR) spectroscopy to analyze binding affinities and conformational changes.

Main Results:

  • The first structure of eIF4E with an m(2,2,7)G-cap was determined, revealing similar binding to m⁷G-cap with a loss of one hydrogen bond.
  • Both nematode and mammalian eIF4E exhibit lower affinity for m(2,2,7)G-cap compared to m⁷G-cap.
  • Binding of m⁷G-cap, m(2,2,7)G-cap, and the m(2,2,7)G-SL RNA induced distinct conformational changes in nematode eIF4E.
  • Specific interactions between Ascaris eIF4E and the SL RNA were observed upon binding the m(2,2,7)G-SL.

Conclusions:

  • Nematode eIF4E binds m(2,2,7)G-cap and m⁷G-cap similarly, but with reduced affinity for the former.
  • Interactions between eIF4E and the SL RNA likely influence translation initiation via eIF4G.
  • These findings highlight the role of 5'-UTRs in mRNA translation and the functional diversity of eIF4E isoforms.