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

Trigger Factor and DnaK possess overlapping substrate pools and binding specificities.

Elke Deuerling1, Holger Patzelt, Sonja Vorderwülbecke

  • 1Zentrum für Molekulare Biologie (ZMBH), Universität Heidelberg, INF282, D-69120 Heidelberg, Germany. e.deuer ling@zmbh.uni-heidelberg.de

Molecular Microbiology
|February 27, 2003
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

SRP orchestrates protein biogenesis beyond initial ER membrane targeting.

Nature communications·2026
Same author

The role of the nucleus in the control of mitochondrial precursor proteins in yeast.

Protein science : a publication of the Protein Society·2026
Same author

Structure-function analysis of the bacterial ClpE-ClpP AAA+ protease.

The Journal of biological chemistry·2026
Same author

Cotranslational Assembly of Oligomeric Proteins.

Annual review of biochemistry·2026
Same author

NAC promotes co-translational protein folding at the ribosomal tunnel exit.

Molecular cell·2026
Same author

Checking in on proteostasis.

Nature structural & molecular biology·2026

Trigger Factor (TF) and DnaK chaperone systems cooperate to fold new proteins in E. coli. They share substrates, with TF having a competitive advantage, and compensate for each other to prevent protein aggregation.

Area of Science:

  • Molecular biology
  • Protein folding mechanisms
  • Bacterial protein homeostasis

Background:

  • Newly synthesized proteins require assistance for proper folding.
  • Ribosome-associated Trigger Factor (TF) and the DnaK chaperone system are key players in E. coli protein folding.
  • Understanding the interplay between these chaperones is crucial for cellular proteostasis.

Purpose of the Study:

  • To investigate the in vivo substrate overlap and functional cooperation between TF and the DnaK chaperone system.
  • To determine how the absence of one chaperone affects the other and cellular protein aggregation.
  • To elucidate the binding specificities and competition dynamics between TF and DnaK for nascent polypeptides.

Main Methods:

  • Generating and analyzing chaperone-deficient E. coli strains (deltatig, DnaK/DnaJ depleted).

Related Experiment Videos

  • Quantifying protein aggregation using temperature shifts and mass spectrometry.
  • Identifying aggregated proteins via mass spectrometry.
  • Screening for chaperone binding sites using peptide libraries.

    • Main Results:

    • TF and DnaK share a common pool of substrates in vivo.
    • Loss of TF leads to significant protein aggregation, especially at higher temperatures, which is partially mitigated by DnaK.
    • Mass spectrometry identified 94 aggregated proteins in TF- and DnaK/DnaJ-depleted cells, including essential cytosolic proteins.
    • TF and DnaK recognize distinct but overlapping binding motifs on substrates, with TF exhibiting competitive binding advantage.

    Conclusions:

    • TF and DnaK cooperate in protein folding by targeting overlapping substrate pools.
    • The cellular heat shock response, inducing DnaK, compensates for the loss of TF.
    • The functional overlap in substrate specificity underlies the cooperative action of these distinct chaperones in maintaining protein homeostasis.