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Related Experiment Videos

Trigger factor retards protein export in Escherichia coli.

Hin C Lee1, Harris D Bernstein

  • 1Genetics and Biochemistry Branch, NIDDK, National Institutes of Health, Bethesda, Maryland 20892, USA.

The Journal of Biological Chemistry
|September 3, 2002
PubMed
Summary
This summary is machine-generated.

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Trigger factor (TF) protein in E. coli binds new polypeptides. TF inactivation accelerates protein export, while TF overproduction retards it, suggesting distinct folding roles from DnaK.

Area of Science:

  • Molecular biology
  • Bacterial protein folding
  • Protein translocation

Background:

  • Trigger factor (TF) is a ribosome-associated chaperone in E. coli.
  • TF interacts with nascent polypeptides and is thought to cooperate with DnaK for protein folding.
  • The precise mechanism of TF-DnaK cooperation remains unclear.

Purpose of the Study:

  • To investigate the function of Trigger factor (TF) in protein export and folding in E. coli.
  • To elucidate the distinct roles of TF and DnaK in protein homeostasis.

Main Methods:

  • Monitoring protein export in E. coli strains with altered TF levels (gene inactivation or overproduction).
  • Assessing the effect of TF manipulation on the export of a cytosolic enzyme fused to a signal peptide.

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Main Results:

  • Inactivation of the TF gene accelerated protein export and reduced the need for targeting factors.
  • Overproduction of TF, but not DnaK, significantly slowed down protein export.
  • Altering TF levels affected the export of signal peptide-fused proteins, indicating TF's role in polypeptide sequestration.

Conclusions:

  • TF uniquely sequesters nascent polypeptides for extended periods.
  • TF and DnaK likely promote protein folding through distinct, complementary mechanisms.