Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Search research articles

Related Experiment Videos

Structure and function in GroEL-mediated protein folding

P B Sigler¹, Z Xu, H S Rye

¹Department of Molecular Biophysics and Biochemistry, School of Medicine, Yale University, New Haven, Connecticut 06510, USA. sigler@csb.yale.edu

Annual Review of Biochemistry

|October 6, 1998

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

Stable transformation of CHO Cells and human NARP cybrids confers oligomycin resistance (oli(r)) following transfer of a mitochondrial DNA-encoded oli(r) ATPase6 gene to the nuclear genome: a model system for mtDNA gene therapy.

Rejuvenation research·2005

Same author

Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding.

Advances in protein chemistry·2002

Same author

ATP-bound states of GroEL captured by cryo-electron microscopy.

Cell·2002

Same author

Protein folding taking shape. Workshop on molecular chaperones.

EMBO reports·2001

Same author

GroEL/GroES-mediated folding of a protein too large to be encapsulated.

Cell·2001

Same author

Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation.

Structure (London, England : 1993)·2001

Same journal

Lactate as a Chemical Modification on Proteins and Metabolites.

Annual review of biochemistry·2026

Same journal

Nucleocytoplasmic Transport.

Annual review of biochemistry·2026

Same journal

Packaging of Single-Stranded RNA in Viruses and Virus-Like Particles.

Annual review of biochemistry·2026

Same journal

Shaping of the Infant Gut Microbiome by Milk Oligosaccharides.

Annual review of biochemistry·2026

Same journal

Proteostasis Deregulation by Metabolism Drives the Hallmarks of Cancer.

Annual review of biochemistry·2026

Same journal

JoAnne Stubbe's Radical Path: A Story of Passion, Curiosity, and Persistence.

Annual review of biochemistry·2026

See all related articles

Chaperonins like GroEL (Hsp60) use ATP and GroES to fold proteins within a sequestered cavity. This mechanism ensures accurate protein expression or recycles misfolded proteins for further attempts.

Area of Science:

Molecular Biology
Biochemistry
Structural Biology

Background:

Protein folding is crucial for accurate genetic information expression.
Chaperonins, such as GroEL (Hsp60), play a vital role in protein folding.
Understanding the GroEL-mediated folding mechanism is essential.

Purpose of the Study:

To elucidate the mechanism of chaperonin (GroEL, Hsp60)-mediated protein folding.
To detail the role of ATP and GroES in the chaperonin folding cycle.
To explain how GroEL facilitates the attainment of native protein states.

Main Methods:

Structural investigations of GroEL-GroES complexes.
Biochemical assays to study protein folding.
Analysis of conformational changes induced by ATP and GroES binding.

Related Experiment Videos

Main Results:

GroEL undergoes major, asymmetric conformational changes upon ATP and GroES binding.
Encapsulation of nonnative polypeptides within GroEL's cavity initiates folding.
ATP hydrolysis and binding drive polypeptide folding and release or recycling.

Conclusions:

The GroEL-GroES system utilizes conformational changes to facilitate protein folding.
This mechanism ensures either the correct folding or the recycling of polypeptides.
The chaperonin system is key to accurate gene expression and protein homeostasis.