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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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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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General Transcription Factors01:30

General Transcription Factors

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Tissue-specific transcription factors contribute to diverse cellular functions in mammals. For example, the gene for beta globin, a major component of hemoglobin, is present in all cells of the body. However, it is only expressed in red blood cells because the transcription factors that can bind to the promoter sequences of the beta globin gene are only expressed in these cells. Tissue-specific transcription factors also ensure that mutations in these factors may impair only the function 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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Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
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A new function and complexity for protein translation initiation factor eIF2B.

Martin D Jennings1, Graham D Pavitt

  • 1a Faculty of Life Sciences ; The University of Manchester ; Manchester , UK.

Cell Cycle (Georgetown, Tex.)
|December 9, 2014
PubMed
Summary
This summary is machine-generated.

The protein eIF2B, crucial for protein synthesis, has a newly discovered role as a GDI displacement factor (GDF). This finding redefines the eIF2 cycling pathway and impacts understanding of Vanishing White Matter disease.

Keywords:
G proteinGAPGDFGDIGEFeIF2Btranslation initiation

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Area of Science:

  • Molecular Biology
  • Protein Synthesis Regulation
  • Neurodegenerative Diseases

Background:

  • eIF2B is a guanine nucleotide exchange factor (GEF) essential for protein synthesis initiation.
  • Its regulation involves eIF2 phosphorylation, and mutations cause leukoencephalopathy with Vanishing White Matter (VWM/CACH).
  • Previous understanding considered eIF2B solely as a GEF.

Purpose of the Study:

  • To elucidate the complete structure and function of the eIF2B complex.
  • To identify new roles of eIF2B in the protein synthesis pathway.
  • To explore the implications for VWM/CACH disease pathogenesis.

Main Methods:

  • Mass spectrometry and cross-linking techniques were employed for structural analysis.
  • Biochemical assays were used to investigate the interaction between eIF2B, eIF2, and eIF5.
  • Literature review of existing findings on eIF2B function and VWM/CACH disease.

Main Results:

  • eIF2B is a decameric complex, a dimer of pentamers, twice the previously estimated size.
  • The eIF2Bγ subunit acts as a GDI displacement factor (GDF), displacing eIF5 from eIF2•GDP.
  • A GTP binding site on eIF2B was identified, suggesting a novel nucleotide exchange mechanism.

Conclusions:

  • eIF2B functions as both a GEF and a GDF, necessitating a revised eIF2 cycling pathway.
  • Structural insights reveal eIF2B's larger-than-expected size and a potential GTP binding site.
  • These findings offer new perspectives on eIF2B regulation and VWM/CACH disease mechanisms.