Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

The Escherichia coli trigger factor

T Hesterkamp1, B Bukau

  • 1Zentrum für Molekulare Biologie, Universität Heidelberg, Germany.

FEBS Letters
|June 24, 1996
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Fragment based drug discovery using fluorescence correlation: spectroscopy techniques: challenges and solutions.

Current topics in medicinal chemistry·2007
Same author

ClpS is an essential component of the N-end rule pathway in Escherichia coli.

Nature·2006
Same author

Low temperature of GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor DnaK.

FEBS letters·2005
Same author

Hsp70 chaperones: cellular functions and molecular mechanism.

Cellular and molecular life sciences : CMLS·2005
Same author

Mechanism of substrate recognition by Hsp70 chaperones.

Biochemical Society transactions·2004
Same author

Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains.

Journal of bacteriology·2004
Same journal

Investigating transcription factor dynamics in health and disease using FRAP.

FEBS letters·2026
Same journal

Regulation of CFTR stability at the plasma membrane-Mechanisms and therapeutic opportunities in cystic fibrosis.

FEBS letters·2026
Same journal

Identification of a Shiga toxin A-derived peptide internalized into Gb3 receptor-bearing cells via interaction with the Shiga toxin B subunit.

FEBS letters·2026
Same journal

The dual role of lectins in cancer-immunotherapy tools and therapeutic targets.

FEBS letters·2026
Same journal

Decoding the dynamic extracellular matrix in cancer-3D models and bioscaffolds rewire the rules of tumor progression.

FEBS letters·2026
Same journal

Extending the classical sequence-structure-function paradigm through protein dynamics and context-dependent behavior.

FEBS letters·2026
See all related articles

E. coli trigger factor, a protein chaperone, assists in folding both cytosolic and secretory proteins. It also works with GroEL to degrade unstable polypeptides.

Area of Science:

  • Molecular Biology
  • Protein Biochemistry
  • Microbiology

Background:

  • E. coli trigger factor is a cytosolic protein.
  • It was initially identified for its role in maintaining secretory protein precursors.
  • Recent research has uncovered new functions for this protein.

Purpose of the Study:

  • To investigate the novel functions of E. coli trigger factor.
  • To explore its role in protein folding and degradation.
  • To understand its involvement with other chaperone systems.

Main Methods:

  • In vitro peptidyl-prolyl cis-trans isomerization assays.
  • Association studies with nascent polypeptide chains (cytosolic and secretory).
  • In vivo studies involving cooperation with the GroEL chaperone for proteolysis.

Related Experiment Videos

Main Results:

  • Trigger factor exhibits peptidyl-prolyl cis-trans isomerase activity, catalyzing protein folding in vitro.
  • It binds to nascent cytosolic and secretory polypeptide chains.
  • Trigger factor collaborates with GroEL to promote the degradation of unstable polypeptides in vivo.

Conclusions:

  • E. coli trigger factor plays a multifaceted role in protein folding.
  • It is involved in the folding of both cytosolic and secretory proteins.
  • Its cooperation with GroEL suggests a role in protein quality control and degradation pathways.