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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

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.
The...
Molecular Chaperones and Protein Folding03:00

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.
The...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
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Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

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Updated: Jun 22, 2026

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
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In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays

Published on: December 29, 2021

Structural characterization of clusterin-chaperone client protein complexes.

Amy R Wyatt1, Justin J Yerbury1, Mark R Wilson1

  • 1School of Biological Sciences, University of Wollongong, Wollongong, New South Wales 2522, Australia.

The Journal of Biological Chemistry
|June 19, 2009
PubMed
Summary
This summary is machine-generated.

Clusterin (CLU) forms large, soluble complexes with client proteins to prevent aggregation. This study characterized these complexes, revealing CLU

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High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis
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High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

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In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
08:16

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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis
09:33

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Chemistry

Background:

  • Clusterin (CLU) is an extracellular chaperone that prevents protein aggregation by forming soluble high molecular weight (HMW) complexes.
  • The physical characteristics of these CLU-client protein complexes were previously unquantified.

Purpose of the Study:

  • To characterize the physical structure of HMW CLU-client protein complexes formed in vitro.
  • To elucidate the mechanism of CLU's chaperone activity at a molecular level.

Main Methods:

  • In vitro complex formation of CLU with citrate synthase (CS), fibrinogen (FGN), and glutathione S-transferase (GST).
  • Analysis using size exclusion chromatography (SEC), SDS-PAGE, dynamic light scattering (DLS), bisANS fluorescence, and circular dichroism (CD) spectrophotometry.

Main Results:

  • HMW CLU-client protein complexes exhibited an approximate 1:2 (CLU:client protein) mass ratio.
  • SEC confirmed complex formation with molecular weights >= 4x10^7 Da.
  • DLS revealed varying diameters for complexes (e.g., HMW CLU-FGN ~108 nm, HMW CLU-CS/GST ~52 nm).
  • BisANS fluorescence indicated CLU prevents hydrophobic region exposure during unfolding.
  • CD analysis suggested CLU interacts with diverse unfolding intermediates.

Conclusions:

  • CLU forms structurally distinct HMW complexes with various client proteins.
  • CLU's chaperone mechanism involves shielding hydrophobic regions, preserving client protein structure.
  • These soluble complexes likely facilitate the clearance of aggregation-prone extracellular proteins in vivo.