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Related Concept Videos

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...
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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.
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Initiation of Translation02:33

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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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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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Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis
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Dynamics of trigger factor interaction with translating ribosomes.

Anna Rutkowska1, Matthias P Mayer, Anja Hoffmann

  • 1Zentrum für Molekulare Biologie Heidelberg, University of Heidelberg, Heidelberg 69120, Germany.

The Journal of Biological Chemistry
|November 30, 2007
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Bacterial trigger factor (TF) chaperone kinetics reveal nascent chains regulate protein folding. Longer chains enhance TF binding and stabilize its interaction with ribosomes, controlling the folding environment.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Protein Folding

Background:

  • Ribosome-associated chaperones, like bacterial trigger factor (TF), are crucial for early protein folding.
  • Understanding the precise mechanisms of chaperone-nascent chain interactions is vital for comprehending protein biogenesis.

Purpose of the Study:

  • To elucidate the kinetic mechanisms governing the ribosome binding and release cycle of bacterial TF.
  • To investigate how nascent chains influence TF's interaction with the ribosome.

Main Methods:

  • Utilized fluorescently labeled chaperone and ribosome-nascent chain complexes.
  • Determined the kinetics of individual steps in the TF-ribosome binding/release cycle.

Main Results:

  • Nascent chain length, sequence, and folding status modulate TF-ribosome association and dissociation rates.
  • TF association rates increase up to 9-fold in the presence of nascent chains, facilitating competition with other chaperones.
  • Longer nascent polypeptides stabilize TF-ribosome complexes, increasing their half-life from 15 to 50 seconds.

Conclusions:

  • Nascent chains actively regulate their own folding environment by modulating ribosome-associated chaperones like TF.
  • TF demonstrates a capacity to bind and accommodate small globular domains within its substrate-binding cavity.
  • These findings provide a kinetic basis for TF's efficient competition for nascent chain binding.