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Related Experiment Videos

Interaction of trigger factor with the ribosome.

Raimund Maier1, Barbara Eckert, Christian Scholz

  • 1Laboratorium für Biochemie, Universität Bayreuth, D-95440 Bayreuth, Germany.

Journal of Molecular Biology
|February 1, 2003
PubMed
Summary

Trigger factor (TF) in Escherichia coli is a chaperone that binds the ribosome to assist protein folding. TF

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Microbiology

Background:

  • Escherichia coli trigger factor (TF) functions as a chaperone and prolyl isomerase.
  • TF interacts with the ribosome to influence the folding of nascent polypeptide chains.
  • Understanding TF's dynamic interactions is crucial for its cellular role.

Purpose of the Study:

  • To investigate the dynamics of trigger factor's interaction with the ribosome.
  • To compare the binding and dissociation kinetics of TF with the ribosome versus unfolded proteins.

Main Methods:

  • Fluorescent labeling of the amino-terminal, ribosome-binding domain of trigger factor.
  • Kinetic analysis of trigger factor-ribosome complex formation and dissociation.

Main Results:

  • Trigger factor association with and dissociation from the ribosome are slow processes.
  • The average lifetime of the trigger factor-ribosome complex is approximately 30 seconds at 20°C.
  • This is significantly longer than the 100 ms lifetime observed for TF-unfolded protein complexes.

Conclusions:

  • The distinct dynamics of TF interactions with the ribosome and protein substrates are essential for its function.
  • Slow binding to the ribosome ensures TF remains associated during protein synthesis.
  • Rapid dissociation from substrates allows efficient scanning for prolyl bonds requiring isomerization.

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