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

Related Concept Videos

Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

Cooperative Binding of Transcription Regulators

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome. Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...

Cooperative Binding of Transcription Regulators

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome. Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

The N-Terminal Domain of LIC12756 Is the Key Determinant of This Protein's Anti-Sigma Activity Toward LIC12757 in Pathogenic <i>Leptospira interrogans</i>.

Pathogens (Basel, Switzerland)·2026

Same author

Cardiomyopathy-associated and basic residue mutations in myopalladin alter actin binding, bundling, and structural stability.

Protein science : a publication of the Protein Society·2026

Same author

Alternative Sigma Factors of RNA Polymerase as Master Regulators in the Pathogenic Spirochaete <i>Leptospira interrogans</i>.

Pathogens (Basel, Switzerland)·2025

Same author

Engineered microRNA scaffolds for potent gene silencing in vivo.

Scientific reports·2025

Same author

Yttrium oxide nanoparticles induce selective cytotoxicity, genomic instability and ROS mitochondrial P53 mediated apoptosis in human pancreatic cancer cells.

Scientific reports·2025

Same author

Evidence for a Putative Regulatory System Consisting of an ECF σ<sup>E</sup>-Type Factor, LIC_12757, and a FecR-like σ Factor Regulator, LIC_12756, in the Pathogenic Spirochaetes <i>Leptospira interrogans</i>.

International journal of molecular sciences·2025

Search research articles

Related Experiment Video

Updated: Jun 18, 2026

Demonstration of Heterologous Complexes formed by Golgi-Resident Type III Membrane Proteins using Split Luciferase Complementation Assay

Demonstration of Heterologous Complexes formed by Golgi-Resident Type III Membrane Proteins using Split Luciferase Complementation Assay

Published on: September 10, 2020

Synergistic cooperation between two ClpB isoforms in aggregate reactivation.

Maria Nagy¹, Izabela Guenther, Vladimir Akoyev

¹Department of Biochemistry, Kansas State University, 141 Chalmers Hall, Manhattan, KS 66506, USA.

Journal of Molecular Biology

|December 8, 2009

Summary

The bacterial AAA+ ATPase ClpB, in both full-length (ClpB95) and truncated (ClpB80) forms, enhances protein aggregate reactivation when working together. This cooperation, possibly via hetero-oligomer formation, improves efficiency beyond individual isoforms.

More Related Videos

CRISPR-Mediated Reorganization of Chromatin Loop Structure

CRISPR-Mediated Reorganization of Chromatin Loop Structure

Published on: September 14, 2018

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

Related Experiment Videos

Last Updated: Jun 18, 2026

Demonstration of Heterologous Complexes formed by Golgi-Resident Type III Membrane Proteins using Split Luciferase Complementation Assay

Demonstration of Heterologous Complexes formed by Golgi-Resident Type III Membrane Proteins using Split Luciferase Complementation Assay

Published on: September 10, 2020

CRISPR-Mediated Reorganization of Chromatin Loop Structure

CRISPR-Mediated Reorganization of Chromatin Loop Structure

Published on: September 14, 2018

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

Area of Science:

Molecular Biology
Protein Biochemistry
Enzymology

Background:

Bacterial AAA+ ATPase ClpB disaggregates proteins by translocating polypeptides.
Two ClpB isoforms exist: full-length ClpB95 and truncated ClpB80, lacking the N-terminal domain.
The specific role of ClpB80 in protein disaggregation remains unclear.

Purpose of the Study:

To investigate the biological role of the truncated ClpB80 isoform.
To determine the functional cooperation between ClpB95 and ClpB80 during protein aggregate reactivation.
To elucidate the mechanism underlying the synergistic activity of ClpB isoforms.

Main Methods:

In vitro and in vivo protein aggregate resolubilization assays.
Analysis of protein binding to aggregated substrates.
Measurement of ATP hydrolysis rates.
Investigation of hetero-oligomer formation between ClpB95 and ClpB80.

Main Results:

ClpB95 and ClpB80 together exhibited higher rates of protein aggregate reactivation than either isoform alone.
The binding of both isoforms to substrates was comparable to individual isoform binding.
ATP hydrolysis and substrate translocation rates were not significantly increased by the combination of isoforms.
ClpB95 and ClpB80 were found to form hetero-oligomers.

Conclusions:

The enhanced reactivation efficiency is attributed to a rate-limiting step post-substrate binding and preceding translocation, which is improved by the presence of both ClpB isoforms.
Hetero-oligomerization between ClpB95 and ClpB80 likely mediates their functional cooperation.
The findings suggest that isoform interaction and cooperation may optimize the function of other AAA+ ATPases.