Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

6.7K
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...
6.7K
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

7.8K
Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high...
7.8K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

7.5K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
7.5K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

8.1K
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...
8.1K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

6.0K
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
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
6.0K
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

5.0K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
5.0K

You might also read

Related Articles

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

Sort by
Same author

From automated Raman to cost-effective nanoparticle-on-film (NPoF) SERS spectroscopy: A combined approach for assessing micro- and nanoplastics released into the oral cavity from chewing gum.

Journal of hazardous materials·2024
Same author

Non-linear responses via agglomeration and aggregation of gold nanoparticles for surface-enhanced Raman spectroscopy (SERS) coupled with chemometric analysis for chlorpyrifos detection.

Food chemistry·2024
Same author

Advancing Mycotoxin Detection in Food and Feed: Novel Insights from Surface-Enhanced Raman Spectroscopy (SERS).

Advanced materials (Deerfield Beach, Fla.)·2024
Same author

Directed Assembly of Au Nanostar@Ag Satellite Nanostructures for SERS-Based Sensing of Hg<sup>2+</sup> Ions.

ACS applied nano materials·2023
Same author

Smartphone-based immunochemical sensor exploiting peroxidase-like activity of ligand-capped gold nanostars: A proof-of-concept detection of Mycobacterium bovis.

Biosensors & bioelectronics·2022
Same author

Peroxidase-Mimicking Activity of Biogenic Gold Nanoparticles Produced from <i>Prunus nepalensis</i> Fruit Extract: Characterizations and Application for the Detection of <i>Mycobacterium bovis</i>.

ACS applied bio materials·2022

Related Experiment Video

Updated: Sep 24, 2025

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes
05:37

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes

Published on: April 4, 2025

866

Parallel G-quadruplex-mediated protein dimerization and activation.

Tuom Tinh Thi Truong1, Cuong Cao2, Dung Thanh Dang1,3

  • 1University of Science, Vietnam National University Ho Chi Minh City Vietnam dung.dthanh@ou.edu.vn.

RSC Advances
|May 6, 2022
PubMed
Summary

Parallel G-quadruplex structures (G4) can induce protein dimerization and activation. This study demonstrates a novel method for observing G4-induced protein functional changes, enhancing caspase 9 activity by 60-fold.

More Related Videos

CD Spectroscopy to Study DNA-Protein Interactions
06:48

CD Spectroscopy to Study DNA-Protein Interactions

Published on: February 10, 2022

7.0K
A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1
11:25

A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1

Published on: March 18, 2017

9.7K

Related Experiment Videos

Last Updated: Sep 24, 2025

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes
05:37

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes

Published on: April 4, 2025

866
CD Spectroscopy to Study DNA-Protein Interactions
06:48

CD Spectroscopy to Study DNA-Protein Interactions

Published on: February 10, 2022

7.0K
A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1
11:25

A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1

Published on: March 18, 2017

9.7K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • G-quadruplexes (G4) are non-canonical DNA secondary structures with diverse biological roles.
  • Protein dimerization and activation are crucial cellular processes often regulated by specific molecular interactions.
  • Understanding G4-protein interactions is key to deciphering their regulatory functions.

Purpose of the Study:

  • To investigate the potential of parallel G-quadruplexes to mediate protein dimerization and activation.
  • To develop a novel FRET-based assay for monitoring G4-induced protein conformational changes.
  • To assess the impact of G4 structures on the enzymatic activity of caspase 9.

Main Methods:

  • Incorporation of a RHAU peptide into a Förster Resonance Energy Transfer (FRET) pair (CFP/YFP) system.
  • Utilizing an apoptotic caspase 9 effector domain.
  • Observing FRET efficiency and caspase 9 cleavage activity in the presence of parallel G4 structures.

Main Results:

  • Significant energy transfer (from CFP to YFP) was observed, indicating protein dimerization.
  • A 60-fold enhancement in caspase 9 cleavage efficiency was detected in the presence of parallel G4.
  • These findings confirm that parallel G4 structures can induce protein dimerization and activation.

Conclusions:

  • Parallel G-quadruplexes can serve as scaffolds to induce protein dimerization and functional activation.
  • The developed FRET-based assay provides a sensitive method for studying G4-protein interactions.
  • This approach has significant potential for investigating G4-targeting functional dimeric proteins in cellular contexts.