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

Catalysis, commitment and encapsulation during GroE-mediated folding.

M Beissinger1, K Rutkat, J Buchner

  • 1Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, Regensburg, 93040, Germany.

Journal of Molecular Biology
|June 17, 1999
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

The Interplay Between Collisionless Magnetic Reconnection and Turbulence.

Space science reviews·2024
Same author

X-ray quasi-periodic eruptions from two previously quiescent galaxies.

Nature·2021
Same author

Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle.

Proceedings of the National Academy of Sciences of the United States of America·2010
Same author

Protein aggregation as a cause for disease.

Handbook of experimental pharmacology·2006
Same author

Hsp70 and Hsp90--a relay team for protein folding.

Reviews of physiology, biochemistry and pharmacology·2004
Same author

Introduction: the cellular protein folding machinery.

Cellular and molecular life sciences : CMLS·2002
Same journal

UPF3A and UPF3B shape the transcriptome cooperatively yet oppose cell function.

Journal of molecular biology·2026
Same journal

Antibody-secreting cells integrate efficient NMD with non‑canonical UPR signaling to maintain proteostasis and support massive immunoglobulin synthesis.

Journal of molecular biology·2026
Same journal

Small molecule stabilization of diverse amyloidogenic immunoglobulin light chains revealed by hydrogen-deuterium exchange mass spectrometry.

Journal of molecular biology·2026
Same journal

UPF1 at Work: Structural and Mechanistic Insights Into a Master Regulator of Nonsense-Mediated mRNA Decay.

Journal of molecular biology·2026
Same journal

Structural basis for the pro-amyloidogenic action and ligand binding of a novel W72R variant of human apolipoprotein A-I.

Journal of molecular biology·2026
Same journal

Cryo-EM Structure of the C. Elegans Septin Tetramer Reveals a Revised Architecture and Conserved Positional Orthology.

Journal of molecular biology·2026
See all related articles

The Escherichia coli GroE chaperone system (GroEL and GroES) aids protein folding, especially under harsh conditions like high temperature or ionic strength. Symmetrical GroE particles are key for efficient refolding of MBP Y283D, often requiring multiple cycles.

Area of Science:

  • Molecular Biology
  • Protein Biochemistry
  • Biophysics

Background:

  • Escherichia coli GroE chaperones (GroEL and GroES) are crucial for protein folding, preventing aggregation and accelerating folding under non-native conditions.
  • The GroE system's function relies on the cooperation between GroEL and GroES, with ATP hydrolysis driving the process.

Purpose of the Study:

  • To analyze the key steps in the interaction of GroE and the maltose-binding protein (MBP) mutant Y283D during catalyzed folding.
  • To investigate the role of environmental conditions (high temperature, high ionic strength) on MBP Y283D folding and GroE's compensatory mechanisms.

Main Methods:

  • Kinetic folding experiments were used to monitor protein refolding dynamics.
  • Electron microscopy was employed to visualize GroE particles and their interaction with substrates.

Related Experiment Videos

Main Results:

  • High temperature and high ionic strength impede MBP Y283D folding, but the complete GroE system (GroEL, GroES, ATP) effectively compensates for this deceleration.
  • Symmetrical GroE particles with GroES bound to both GroEL ends are critical for efficient MBP Y283D refolding at elevated temperatures.
  • While MBP Y283D folding can initiate in one cycle, multiple cycles of GroE interaction are typically needed to achieve the native state due to low commitment after a single ATP hydrolysis cycle.

Conclusions:

  • The GroE chaperone system actively catalyzes protein folding, particularly under restrictive conditions.
  • The structural configuration of GroE, specifically symmetrical particles, enhances chaperone efficiency.
  • Repeated cycles of GroE-mediated protein encapsulation and release are necessary for complete and stable protein refolding.