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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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Translational Regulation01:29

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Translational regulation in prokaryotes ensures efficient protein synthesis by controlling ribosome access to mRNA. This regulation is mediated by secondary RNA structures, including translational riboswitches, RNA thermometers, and small RNAs (sRNAs), which respond to intracellular and environmental signals to modulate gene expression.Translational RiboswitchesRiboswitches in the leader region of mRNAs can regulate translation by altering the accessibility of the Shine-Dalgarno (SD) sequence,...
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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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Chromatin Structure Regulates pre-mRNA Processing02:41

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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.
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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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Nonsense-mediated mRNA Decay02:27

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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.
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Related Experiment Video

Updated: Aug 12, 2025

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
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Neuronal RNA-Binding Protein HuD Interacts with Translation Initiation Factor eIF3.

Hikari Nishisaka1, Takumi Tomohiro1, Akira Fukao1

  • 1Department of Pharmacy, Kindai University.

Biological & Pharmaceutical Bulletin
|February 1, 2023
PubMed
Summary

The neuronal RNA-binding protein HuD interacts with eukaryotic initiation factor 3 (eIF3), specifically the eIF3b subunit. This interaction enhances translation initiation efficiency, crucial for protein synthesis and cellular functions.

Keywords:
RNA-binding proteineukaryotic translation initiation factortranslational control

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Translation initiation is a key regulatory step in protein synthesis.
  • RNA-binding proteins (RBPs) control translation and are vital for cell functions.
  • HuD, a neuronal RBP, was previously shown to enhance translation via eIF4A and poly(A) tail interactions.

Purpose of the Study:

  • To elucidate the mechanism by which HuD regulates translation initiation.
  • To identify novel interaction partners of HuD involved in translation control.

Main Methods:

  • In vitro binding assays to test interactions between HuD and eIF3 subunits.
  • Analysis of conserved regions within Hu proteins.

Main Results:

  • HuD directly binds to the eIF3b subunit of eukaryotic initiation factor 3 (eIF3).
  • The linker region of HuD is essential for this interaction with eIF3b.
  • The eIF3b-binding domain in HuD is conserved across the Hu protein family (HuB, HuC, HuD, HuR).

Conclusions:

  • HuD's interaction with eIF3b likely stabilizes the translation initiation complex, enhancing translation efficiency.
  • This interaction provides a new mechanism for HuD-mediated translation regulation.
  • The conserved binding region suggests a common mechanism for translation stimulation by Hu proteins.