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

GroEL/S substrate specificity based on substrate unfolding propensity.

Kristin N Parent1, Carolyn M Teschke

  • 1Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269, USA.

Cell Stress & Chaperones
|April 20, 2007
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

A highly conserved basic motif in the wing domain of portal protein is necessary for oligomerization and incorporation in phage P22.

Journal of virology·2026
Same author

Encapsulation in a Bacterial Microcompartment Shell Improves Thermal Stability of a Glycolytic Enzyme.

ACS synthetic biology·2026
Same author

Many paths, similar destinations: viruses and bacterial microcompartments form polyhedra inside cells.

Journal of virology·2026
Same author

Screening metatranscriptomes for ultrastable RNA secondary structures reveals hidden bacteriophages and novel capsid nanomaterials.

bioRxiv : the preprint server for biology·2026
Same author

The <i>Shigella</i> siphophage Sf11 tail structure and host attachment mechanism.

Journal of virology·2025
Same author

Structures of two LarA-like nickel-pincer nucleotide cofactor-utilizing enzymes with a single catalytic histidine residue.

Protein science : a publication of the Protein Society·2025
Same journal

Hspa1b Attenuates Hypoxia/reoxygenation-induced Cardiomyocyte Injury Through Dual Suppression of P53-driven Apoptotic and Ferroptotic Pathways.

Cell stress & chaperones·2026
Same journal

Evolution of Hsp90 targeting: From stress biology to clinical translation.

Cell stress & chaperones·2026
Same journal

Insights into the function and structure of the R2TP (RUVBL1-RUVBL2-RPAP3-PIH1D1)chaperone complex.

Cell stress & chaperones·2026
Same journal

Wiring of cellular proteostasis by J-domain proteins.

Cell stress & chaperones·2026
Same journal

Hsp90: A means to an end.

Cell stress & chaperones·2026
Same journal

Ninth BHD International Symposium: Advancing research through global collaboration.

Cell stress & chaperones·2026
See all related articles

A new mutation in P22 phage coat protein (F170L) restores normal folding and assembly, reducing the need for GroEL/S chaperones. This finding offers insights into protein folding and phage assembly mechanisms.

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Phage P22 wild-type (WT) coat protein folds independently, but temperature-sensitive-folding (tsf) variants require GroEL/S chaperones.
  • Assembly into procapsids requires the P22 scaffolding protein for all coat protein variants.
  • A previous suppressor (su) substitution, T1661, rescued tsf variants by inducing GroEL/S, favoring correct folding and assembly.

Purpose of the Study:

  • Investigate the folding and assembly of P22 coat protein variants with the F170L suppressor substitution.
  • Determine the role of the F170L substitution in GroEL/S chaperone dependence and procapsid formation.
  • Elucidate the mechanism by which F170L restores wild-type-like properties to tsf coat proteins.

Main Methods:

  • Monitoring phage production with dysfunctional GroEL.

Related Experiment Videos

  • Circular dichroism and tryptophan fluorescence spectroscopy.
  • Native acrylamide gel electrophoresis.

    • Main Results:

    • tsf:F170L coat proteins showed a reduced requirement for GroEL/S and did not induce chaperone production.
    • Spectroscopic and electrophoretic analyses indicated restoration of WT-like native state and increased stability for tsf:F170L proteins.
    • Procapsid production was enhanced in tsf:F170L variants compared to their tsf parents.

    Conclusions:

    • The F170L suppressor substitution restores tsf coat proteins to a WT-like state, decreasing their dependence on GroEL/S chaperones.
    • The findings suggest that GroEL/S can be induced by increasing the population of unfolding intermediates.
    • This study provides a deeper understanding of chaperone function in protein folding and viral assembly.