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FIBS-enabled Noninvasive Metabolic Profiling
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Real-time observation of trigger factor function on translating ribosomes.

Christian M Kaiser1, Hung-Chun Chang, Vishwas R Agashe

  • 1Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany.

Nature
|October 20, 2006
PubMed
Summary

Trigger factor (TF) is a bacterial chaperone that interacts dynamically with ribosomes and nascent polypeptides during protein synthesis. Its binding duration correlates with polypeptide aggregation propensity, preventing misfolding.

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Area of Science:

  • Molecular biology
  • Protein folding
  • Bacterial protein synthesis

Background:

  • Co-translational chaperone functions are crucial for protein folding but remain poorly understood.
  • Trigger factor (TF) is the initial molecular chaperone interacting with nascent polypeptides in bacteria.

Purpose of the Study:

  • To elucidate the dynamic interaction cycle of ribosome-associated TF with translating polypeptides.
  • To understand how TF prevents protein misfolding during translation.

Main Methods:

  • Real-time fluorescence spectroscopy was employed to monitor TF function and structural changes.
  • Investigated TF interactions with ribosomes and nascent chains.

Main Results:

  • TF exhibits a dynamic reaction cycle with ribosomes, stabilizing in an open, activated conformation upon binding.
  • Activated TF has a mean residence time of ~10 s at the ribosome but can associate with nascent chains for up to 35 s.
  • The duration of TF-nascent chain interaction is linked to hydrophobic motifs and aggregation propensity of the polypeptide.

Conclusions:

  • TF's dynamic interaction cycle and residence time explain its role in preventing co-translational misfolding.
  • Findings suggest a regulatory paradigm for nucleotide-independent chaperones.