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Molecular Chaperones and Protein Folding

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Molecular Chaperones and Protein Folding

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Related Experiment Video

Updated: May 29, 2026

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Published on: June 7, 2020

Chaperonins facilitate KNOTTED1 cell-to-cell trafficking and stem cell function.

Xianfeng Morgan Xu¹, Jing Wang, Zhenyu Xuan

¹Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.

Science (New York, N.Y.)

|August 27, 2011

Summary

Chaperonin complexes are vital for plant stem cell maintenance by facilitating the cell-to-cell trafficking of KNOTTED1 (KN1) homeobox (KNOX) transcription factors through plasmodesmata.

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In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

Area of Science:

Plant biology
Molecular plant science
Cell biology

Background:

Plant cell-to-cell communication relies on selective molecule trafficking via plasmodesmata.
KNOTTED1 (KN1) homeobox (KNOX) transcription factors are crucial for maintaining plant stem cell populations.

Purpose of the Study:

To investigate the role of chaperonins in the trafficking and function of KNOX transcription factors.
To elucidate the mechanism by which chaperonins support plant stem cell maintenance.

Main Methods:

Genetic interaction studies to identify functional relationships.
Physical interaction assays to confirm protein complex formation.
Tissue-specific complementation assays to assess protein function in vivo.

Main Results:

Chaperonin complexes are required for the cell-to-cell trafficking of KNOX transcription factors.
Genetic and physical evidence demonstrates a functional link between chaperonins and KNOX-dependent stem cell maintenance.
Chaperonins facilitate post-translational protein refolding essential for trafficking.

Conclusions:

Chaperonins are essential for the trafficking of specific mobile transcription factors in plants.
Chaperonin-mediated protein trafficking is critical for the proper function of plant stem cells.