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

Nucleosome Remodeling02:54

Nucleosome Remodeling

8.7K
Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
8.7K
Long-patch Base Excision Repair01:02

Long-patch Base Excision Repair

6.3K
Since the discovery of the two BER pathways, there has been a debate about how a cell chooses one pathway over the other and the factors determining this selection. Numerous in vitro experiments have pointed out multiple determinants for the sub-pathway selection. These are:
6.3K
Restarting Stalled Replication Forks02:37

Restarting Stalled Replication Forks

5.1K
DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart,...
5.1K
Rab Cascades01:25

Rab Cascades

2.8K
Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
2.8K

You might also read

Related Articles

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

Sort by
Same author

Covalent Modification of Keap1 by the Key Metabolic Cofactor Coenzyme A Under Oxidative and Metabolic Stress.

Antioxidants (Basel, Switzerland)·2026
Same author

Modulation of islet amyloid polypeptide induced β-cell toxicity and amyloid formation by serum albumin proteins.

Biophysical chemistry·2026
Same author

Co-expression of the RPS6KB1 and PDPK1 genes for production of activated p70S6K1 using bac-to-bac baculovirus expression system.

Molecular biology reports·2025
Same author

The islet tissue plasminogen activator/plasmin system is upregulated with human islet amyloid polypeptide aggregation and protects beta cells from aggregation-induced toxicity.

Diabetologia·2024
Same author

Investigating the Regulation of Ribosomal Protein S6 Kinase 1 by CoAlation.

International journal of molecular sciences·2024
Same author

The processing intermediate of human amylin, pro-amylin(1-48), has in vivo and in vitro bioactivity.

Biophysical chemistry·2024

Related Experiment Video

Updated: May 5, 2026

Genome-wide Mapping of Protein-DNA Interactions with ChEC-seq in Saccharomyces cerevisiae
10:43

Genome-wide Mapping of Protein-DNA Interactions with ChEC-seq in Saccharomyces cerevisiae

Published on: June 3, 2017

10.5K

Dissecting the Interplay Between NRF2 and BACH1 at CsMBEs.

Maria-Armineh Tossounian1, Alexander Zhyvoloup1, Rakesh Chatterjee2

  • 1Structural and Molecular Biology Department, University College London, London WC1E 6BT, UK.

Antioxidants (Basel, Switzerland)
|October 29, 2025
PubMed
Summary
This summary is machine-generated.

Transcription factors BACH1 and NRF2 regulate gene expression by competing for DNA binding. A novel system revealed that redox changes impact BACH1 binding, facilitating rapid gene regulation switches.

Keywords:
BACH1NRF2bZIPprotein-DNA interactionsredox regulation

More Related Videos

Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using χCRAC
09:15

Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using χCRAC

Published on: May 9, 2020

6.1K
Genome-wide Profiling of Transcription Factor-DNA Binding Interactions in Candida albicans: A Comprehensive CUT&RUN Method and Data Analysis Workflow
07:48

Genome-wide Profiling of Transcription Factor-DNA Binding Interactions in Candida albicans: A Comprehensive CUT&RUN Method and Data Analysis Workflow

Published on: April 1, 2022

3.3K

Related Experiment Videos

Last Updated: May 5, 2026

Genome-wide Mapping of Protein-DNA Interactions with ChEC-seq in Saccharomyces cerevisiae
10:43

Genome-wide Mapping of Protein-DNA Interactions with ChEC-seq in Saccharomyces cerevisiae

Published on: June 3, 2017

10.5K
Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using χCRAC
09:15

Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using χCRAC

Published on: May 9, 2020

6.1K
Genome-wide Profiling of Transcription Factor-DNA Binding Interactions in Candida albicans: A Comprehensive CUT&RUN Method and Data Analysis Workflow
07:48

Genome-wide Profiling of Transcription Factor-DNA Binding Interactions in Candida albicans: A Comprehensive CUT&RUN Method and Data Analysis Workflow

Published on: April 1, 2022

3.3K

Area of Science:

  • Molecular Biology
  • Gene Regulation
  • Biochemistry

Background:

  • BACH1 and NRF2 are transcription factors regulating antioxidant and iron metabolism genes.
  • They compete for cis-regulatory Maf-binding elements (CsMBEs) as heterodimers with small Maf proteins (sMafs).

Purpose of the Study:

  • To dissect the mechanisms underlying BACH1 and NRF2 competition for DNA binding.
  • To investigate the role of redox sensitivity in regulating transcriptional switches.

Main Methods:

  • Development of a chimeric tethering system linking DNA-binding domains of BACH1 or NRF2 to sMafG.
  • Site-specific fluorescent labeling of proteins for tracking complex compositions.
  • Electrophoretic mobility shift assays (EMSAs) and competition assays.

Main Results:

  • BACH1/sMafG and NRF2/sMafG heterodimers bind CsMBEs with similar affinities.
  • BACH1 DNA binding is redox-sensitive and C574-dependent, promoting partner exchange.
  • BACH1 and NRF2 can displace each other from DNA, more efficiently as preassembled heterodimers.

Conclusions:

  • A redox-sensitive mechanism regulates transcriptional switches at CsMBEs.
  • Preformed heterodimers facilitate rapid displacement of transcription factors at target promoters.