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

Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

16.7K
For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
16.7K
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

15.0K
The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
15.0K
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

5.6K
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...
5.6K
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

7.3K
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...
7.3K
DNA Helicases00:55

DNA Helicases

24.1K
DNA unwinding helicase enzymes are a type of motor protein. Motor proteins can translocate along filaments or polymers using energy generated from ATP hydrolysis. Helicases are involved in all the important cellular processes where DNA unwinding is required, such as DNA replication, repair, recombination, and transcription. They are present in all living organisms, but vary in their structure, function, and mechanism of action. For example, in prokaryotes, DnaB helicase binds and translocates...
24.1K
Ligand Binding Sites02:40

Ligand Binding Sites

15.0K
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
15.0K

You might also read

Related Articles

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

Sort by
Same author

The schizophrenia associated protein DISC1 forms a multivalent tetrameric hub via conserved UVR dimers.

Nature communications·2026
Same author

Rational discovery of therapeutic PAK1 allosteric activators.

Cell·2026
Same author

Deep Learning-Based Event Classification of Mass Photometry Data for Optimal Mass Measurement at the Single-Molecule Level.

ACS nano·2026
Same author

Molecular basis for CSB stimulation of the SNM1A DNA repair nuclease.

Research square·2025
Same author

Best practice mass photometry: a guide to optimal single-molecule mass measurement.

Nature protocols·2025
Same author

Programmable DNA shell scaffolds for directional membrane budding.

Nature communications·2025
Same journal

A Domino-Synthesized Dicoordinate Copper(I) Bis-imidazopyridine Complex Triggering Cuproptosis/Ferroptosis for Enhanced Cancer Immunotherapy.

Angewandte Chemie (International ed. in English)·2026
Same journal

Mirror-Symmetric Organic Two-Dimensional Crystals for Alternative Photon Transport Pathways.

Angewandte Chemie (International ed. in English)·2026
Same journal

Cobalt-Catalyzed Migratory E-Selective Asymmetric Aza-Nozaki-Hiyama-Kishi Coupling.

Angewandte Chemie (International ed. in English)·2026
Same journal

Facile Synthesis of α,ω-Dihydroxy Telechelic Macromonomers From Ethylene and α-Olefins for Recyclable Alternating Block Copolymers.

Angewandte Chemie (International ed. in English)·2026
Same journal

Multi-Atom Sub-Nanometer Assemblies on Interpenetrating Multi-Chambered N/C Nanospheres.

Angewandte Chemie (International ed. in English)·2026
Same journal

A Synergistic C<sub>2+</sub> Alcohols/Olefins-Intermediated Pathway Boosts CO<sub>2</sub> Hydrogenation to Aromatics.

Angewandte Chemie (International ed. in English)·2026
See all related articles

Related Experiment Video

Updated: Jan 27, 2026

Visualization of Surface-tethered Large DNA Molecules with a Fluorescent Protein DNA Binding Peptide
08:51

Visualization of Surface-tethered Large DNA Molecules with a Fluorescent Protein DNA Binding Peptide

Published on: June 23, 2016

11.2K

Dissecting FOXP2 Oligomerization and DNA Binding.

Katharina Häußermann1, Gavin Young2, Philipp Kukura2

  • 1Physik Department & Munich School of Bioengineering, Technische Universität München, Am Coulombwall 4a, 85784, Garching, Germany.

Angewandte Chemie (International Ed. in English)
|March 20, 2019
PubMed
Summary
This summary is machine-generated.

Forkhead box protein P2 (FOXP2) dimerization is mediated by its leucine zipper domain, which also aids DNA binding. The forkhead domain is crucial for DNA binding, while the zinc finger domain influences dimerization.

Keywords:
FOXP2biochipsmass photometryprotein-DNA interactionsprotein-protein interactions

More Related Videos

Methyl-binding DNA capture Sequencing for Patient Tissues
08:40

Methyl-binding DNA capture Sequencing for Patient Tissues

Published on: October 31, 2016

9.0K
DNA-magnetic Particle Binding Analysis by Dynamic and Electrophoretic Light Scattering
10:35

DNA-magnetic Particle Binding Analysis by Dynamic and Electrophoretic Light Scattering

Published on: November 9, 2017

12.5K

Related Experiment Videos

Last Updated: Jan 27, 2026

Visualization of Surface-tethered Large DNA Molecules with a Fluorescent Protein DNA Binding Peptide
08:51

Visualization of Surface-tethered Large DNA Molecules with a Fluorescent Protein DNA Binding Peptide

Published on: June 23, 2016

11.2K
Methyl-binding DNA capture Sequencing for Patient Tissues
08:40

Methyl-binding DNA capture Sequencing for Patient Tissues

Published on: October 31, 2016

9.0K
DNA-magnetic Particle Binding Analysis by Dynamic and Electrophoretic Light Scattering
10:35

DNA-magnetic Particle Binding Analysis by Dynamic and Electrophoretic Light Scattering

Published on: November 9, 2017

12.5K

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Protein-protein and protein-substrate interactions are vital for biological functions.
  • Understanding these interactions is challenging due to complex regulatory factors.
  • The transcription factor forkhead box protein P2 (FOXP2) has domains involved in DNA binding and oligomerization, but their specific roles are unclear.

Purpose of the Study:

  • To characterize the DNA binding and protein oligomerization of FOXP2.
  • To elucidate the specific roles of the leucine zipper (LZ) and C2H2-zinc finger (ZF) domains in FOXP2 function.
  • To understand the molecular mechanisms underlying FOXP2's transcriptional activity.

Main Methods:

  • A combined biochemical and biophysical approach was employed.
  • Electrically switchable DNA biochips were utilized for interaction studies.
  • Single-molecule mass analysis was performed to characterize protein behavior.

Main Results:

  • The leucine zipper (LZ) domain mediates FOXP2 dimerization through coiled-coil formation and also contributes to DNA binding.
  • The C2H2-zinc finger (ZF) domain assists in protein dimerization when the LZ coiled-coil is intact but is not involved in DNA binding.
  • The forkhead domain (FHD) was identified as the primary domain responsible for DNA binding.

Conclusions:

  • The study clarifies the distinct roles of FOXP2's structural domains in DNA binding and dimerization.
  • FOXP2 dimerization is a complex process involving both the LZ and ZF domains.
  • The findings provide critical insights into the molecular mechanisms governing FOXP2 transcriptional regulation.