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Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

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

Molecular Chaperones and Protein Folding

Cotranslational Protein Translocation

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...

Bacterial Protein Maturation

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Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...

Protein Translocation Machinery on the ER Membrane

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...

Protein Transport to the Stroma

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Chloroplasts are triple membrane structures with an outer membrane, an inner membrane, and a thylakoid membrane, each containing distinct metabolite transporters, membrane translocons, and enzymes. Appropriate sorting and translocating these proteins to their correct membrane systems is essential for chloroplast function.
Protein complexes called the translocon of the outer chloroplast membrane or TOC complex, and the translocon of the inner chloroplast membrane or TIC complex mediate the...

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Related Experiment Video

Updated: Dec 30, 2025

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

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Published on: June 7, 2018

TRiC/CCT Chaperonin: Structure and Function.

Mingliang Jin¹, Caixuan Liu¹, Wenyu Han¹

¹National Center for Protein Science Shanghai, State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Shanghai, China.

Sub-Cellular Biochemistry

|January 16, 2020

Summary

This summary is machine-generated.

The TRiC/CCT chaperonin is vital for protein folding and homeostasis. Its dysfunction is linked to diseases like cancer, highlighting its therapeutic potential.

Keywords:

ATP-driven conformational changes Chaperonin Cryo-EM Function Structure Substrate folding TRiC/CCT

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Area of Science:

Molecular Biology
Cell Biology
Biochemistry

Background:

The eukaryotic group II chaperonin, TRiC/CCT, is crucial for folding approximately 10% of cytosolic proteins, including essential structural and regulatory proteins.
TRiC/CCT plays a critical role in maintaining cellular protein homeostasis, and its malfunction is implicated in human diseases such as cancer and neurodegenerative disorders.
Composed of eight paralogous subunits, TRiC/CCT functions as a complex macromolecular machine, with each subunit contributing to assembly, allosteric cooperativity, substrate recognition, and protein folding.

Purpose of the Study:

To review recent advancements in understanding the structure, subunit arrangement, conformational cycle, and substrate folding mechanisms of TRiC/CCT.
To explore the connection between TRiC/CCT (both oligomeric and monomeric forms) and various human diseases.
To discuss the potential therapeutic applications of targeting TRiC/CCT in disease treatment.

Main Methods:

Literature review of recent research on TRiC/CCT structure and function.
Analysis of studies linking TRiC/CCT dysfunction to disease pathogenesis.
Exploration of emerging therapeutic strategies targeting TRiC/CCT.

Main Results:

Significant progress has been made in elucidating the structural intricacies and conformational dynamics of TRiC/CCT.
Evidence increasingly links TRiC/CCT aberrations to the development and progression of diseases.
TRiC/CCT's role in protein homeostasis is confirmed, with its dysfunction impacting cellular health.

Conclusions:

TRiC/CCT is a central player in protein folding and cellular health.
Dysfunctional TRiC/CCT is a significant factor in various human diseases.
Targeting TRiC/CCT presents promising therapeutic avenues for treating related diseases.