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 Experiment Videos

RFX1, a single DNA-binding protein with a split dimerization domain, generates alternative complexes

Y Katan-Khaykovich1, Y Shaul

  • 1Department of Molecular Genetics, The Weizmann Institute of Science, Rehovot 76100, Israel.

The Journal of Biological Chemistry
|September 12, 1998
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Co-expression of fibulin-5 and VEGF165 increases long-term patency of synthetic vascular grafts seeded with autologous endothelial cells.

Gene therapy·2015
Same author

The polyomavirus middle T-antigen oncogene activates the Hippo pathway tumor suppressor Lats in a Src-dependent manner.

Oncogene·2014
Same author

c-Abl antagonizes the YAP oncogenic function.

Cell death and differentiation·2014
Same author

AMPK couples p73 with p53 in cell fate decision.

Cell death and differentiation·2014
Same author

The Hippo pathway kinase Lats2 prevents DNA damage-induced apoptosis through inhibition of the tyrosine kinase c-Abl.

Cell death and differentiation·2013
Same author

Dendritic cells and their role in periodontal disease.

Oral diseases·2013
Same journal

Isotope-Edited ESEEM: A New Method for Probing Copper Binding Sites in Neurodegenerative Proteins.

The Journal of biological chemistry·2026
Same journal

Introduction to the Thematic Review Series on Intracellular Protein Degradation. The ubiquitous biology of intracellular protein degradation: a tribute to Alfred L. ("Fred") Goldberg.

The Journal of biological chemistry·2026
Same journal

Correction: Aromatic residue-rich amino-terminal segments of temporin L self-assemble into collagen-mimetic peptides with cell-adhesion properties.

The Journal of biological chemistry·2026
Same journal

YhbO is a DJ-1 family glyoxalase and α-oxoaldehyde hydratase that confers resistance to reactive carbonyl stress (112).

The Journal of biological chemistry·2026
Same journal

ARMH3 acts as a central scaffold at the Golgi/TGN through interactions with Arl5, GBF1, and PI4KB.

The Journal of biological chemistry·2026
Same journal

PAX8 controls proximal tubule epithelial identity and stress response through epigenetic modification of distal regulatory elements.

The Journal of biological chemistry·2026
See all related articles

The transcription regulator RFX1 forms distinct DNA-protein complexes. Its extended dimerization domain controls complex formation and influences gene transcription by mediating alternative homodimeric interactions.

Area of Science:

  • Molecular Biology
  • Gene Regulation
  • Virology

Background:

  • Viral and cellular gene transcription is regulated by DNA sites similar to the hepatitis B virus enhancer EP element.
  • These sites form DNA-protein complexes, with the upper EP complex involving homodimers of the transcription regulator RFX1.

Purpose of the Study:

  • To investigate the structure and function of the RFX1 dimerization domain.
  • To understand how RFX1 mediates the formation of different DNA-protein complexes and regulates transcription.

Main Methods:

  • Analysis of RFX1 deletions within its extended dimerization domain.
  • Characterization of DNA-protein complex formation using palindromic and nonpalindromic DNA sites.
  • Correlation of complex formation with transcriptional activity.

Related Experiment Videos

Main Results:

  • RFX1 possesses a split, extended dimerization domain with conserved boxes.
  • RFX1 forms two distinct DNA-protein complexes: a previously characterized one and a novel, low-mobility complex with palindromic sites.
  • Deletions in the dimerization domain altered the ratio of these complexes, impacting transcriptional repression.

Conclusions:

  • The extended RFX1 dimerization domain mediates the formation of alternative homodimeric complexes through varied intersubunit interactions.
  • This mechanism allows RFX1 to regulate the abundance of different complexes, thereby controlling transcriptional activity.