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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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Improving Translational Accuracy02:07

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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

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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

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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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Ribosomal RNA Synthesis02:53

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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.
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Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
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Crystal structure of eukaryotic translation initiation factor 2B.

Kazuhiro Kashiwagi1,2,3, Mari Takahashi3, Madoka Nishimoto3

  • 1Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.

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|February 23, 2016
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Summary

Scientists determined the structure of eukaryotic translation initiation factor 2B (eIF2B), revealing how stress-induced phosphorylation of eIF2α creates a nonproductive complex, inhibiting protein synthesis. This provides insight into cellular stress responses.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cellular Biology

Background:

  • Eukaryotic cells regulate protein synthesis during stress by inhibiting eukaryotic translation initiation factor 2B (eIF2B).
  • eIF2B acts as a guanine nucleotide exchange factor for eIF2, crucial for initiating protein synthesis.
  • Stress-induced phosphorylation of eIF2α inhibits eIF2B activity, a key mechanism in translational control.

Purpose of the Study:

  • To determine the three-dimensional structure of the eIF2B complex.
  • To elucidate the structural basis for the inhibition of eIF2B by phosphorylated eIF2α.
  • To provide a structural framework for understanding stress-induced translational control.

Main Methods:

  • X-ray crystallography was used to determine the structure of the Schizosaccharomyces pombe eIF2B complex.
  • Structure-based in vitro analysis, including surface-scanning site-directed photo-cross-linking, identified binding interfaces.
  • A structural model of the eIF2B-phosphorylated eIF2α complex was constructed.

Main Results:

  • The crystal structure revealed an unprecedented arrangement of the eIF2B heterodecamer, with a hexameric regulatory subcomplex binding two catalytic subcomplexes.
  • eIF2α-binding and eIF2γ-binding interfaces were identified on distinct subcomplexes.
  • Phosphorylated eIF2α binds more strongly to eIF2B, forming a nonproductive complex that inhibits nucleotide exchange on eIF2γ.

Conclusions:

  • The determined structure provides a detailed molecular understanding of eIF2B architecture.
  • Stress-induced phosphorylation of eIF2α leads to the formation of a nonproductive eIF2-eIF2B complex, halting nucleotide exchange.
  • This study offers a structural basis for the eIF2B-mediated regulation of protein synthesis under cellular stress.