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Trigger factor accelerates nascent chain compaction and folding.

Katharina Till1, Anne-Bart Seinen1, Florian Wruck1

  • 1AMOLF, Amsterdam 1098 XG, Netherlands.

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Summary
This summary is machine-generated.

The trigger factor chaperone accelerates nascent chain folding directly on the ribosome. This cotranslational folding impacts protein assembly and aggregation.

Keywords:
chaperonesoptical tweezersprotein foldingribosomes

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Area of Science:

  • Molecular Biology
  • Biophysics

Background:

  • Nascent chain conformational control at the ribosome is poorly understood.
  • Chaperones typically act away from the ribosome, but protein folding challenges occur during translation.

Purpose of the Study:

  • To investigate the role of the Escherichia coli chaperone trigger factor (TF) in nascent chain conformational control at the ribosome.
  • To elucidate the mechanisms by which TF influences protein folding during translation.

Main Methods:

  • Selective ribosome profiling combined with optical tweezers and single-molecule fluorescence.
  • Utilized dihydrofolate reductase (DHFR) as a model system.

Main Results:

  • Trigger factor (TF) was shown to accelerate nascent chain folding on the ribosome.
  • TF exhibits transient scanning followed by stable binding as the nascent chain folds and collapses.
  • TF binding induces nascent chain collapse and stabilizes partial folds, with compaction prolonging TF binding.
  • TF-accelerated folding is dependent on the emergence of specific peptide segments crucial for protein structure.

Conclusions:

  • Trigger factor plays a critical role in facilitating cotranslational folding at the ribosome.
  • TF-mediated folding acceleration influences cotranslational protein assembly, aggregation, and translational pausing.
  • These findings suggest TF's importance in protein biogenesis across life.