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

The dimerization domain upstream binding factor contains multiple helical structures

Y S Lai1, H B Tseng, C H Hu

  • 1Institute of Marine Biology, National Taiwan Ocean University, R.O.C.

Biochemical and Biophysical Research Communications
|March 27, 1996
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

Spatial correlation at the boson peak frequency in amorphous materials.

Nature communications·2025
Same author

Erratum: Centrality-Dependent Modification of Jet-Production Rates in Deuteron-Gold Collisions at sqrt[s_{NN}]=200  GeV [Phys. Rev. Lett. 116, 122301 (2016)].

Physical review letters·2025
Same author

[A preliminary study on the causes of olfactory dysfunction following aesthetic rhinoplasty].

Zhonghua er bi yan hou tou jing wai ke za zhi = Chinese journal of otorhinolaryngology head and neck surgery·2025
Same author

[Diagnostic value of Gd-EOB-DTPA-enhanced MRI radiomics models for dual-phenotype hepatocellular carcinoma].

Zhonghua yi xue za zhi·2024
Same author

[Effectiveness and safety of multimodal analgesia in open gastrostomy in patients with end-stage head and neck cancer].

Zhonghua yi xue za zhi·2024
Same author

ψ(2S) Suppression in Pb-Pb Collisions at the LHC.

Physical review letters·2024
Same journal

Biosynthesis, characterization and biological potential of microbe-mediated silver nanoparticles using thermophilic actinomycetes, Streptomyces nigra.

Biochemical and biophysical research communications·2026
Same journal

COP9 signalosome 8 mediated autophagy drives proliferation, invasion, and metastasis in pancreatic ductal adenocarcinoma.

Biochemical and biophysical research communications·2026
Same journal

Tumor budding in colorectal cancer: partial EMT, microenvironmental remodeling, and metastatic competence.

Biochemical and biophysical research communications·2026
Same journal

Exploring the therapeutic versatility and multitarget pharmacological potential of acyl hydrazone-hydrazide scaffolds.

Biochemical and biophysical research communications·2026
Same journal

The plasma membrane H<sup>+</sup>-ATPase OSA2 negatively regulates salt tolerance in rice seedlings.

Biochemical and biophysical research communications·2026
Same journal

MiR-425-5p modulation of CREB1 affects inflammatory response and motor recovery after spinal cord injury.

Biochemical and biophysical research communications·2026
See all related articles

Upstream binding factor (UBF) homodimerization, crucial for RNA polymerase I transcription, is mediated by hydrophobic interactions within its dimerization domain. This study reveals how these interactions drive UBF association and DNA binding.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Upstream binding factor (UBF) is a key transcription factor for RNA polymerase I.
  • Active UBF functions as a homodimer, facilitated by its N-terminal dimerization domain.

Purpose of the Study:

  • To investigate the molecular mechanisms underlying UBF homodimerization.
  • To determine the role of the UBF dimerization domain in protein-protein and protein-DNA interactions.

Main Methods:

  • Expression and purification of a recombinant UBF fragment (dbUBF) containing dimerization and DNA-binding domains.
  • In vitro dimerization assays.
  • Gel retardation assays to assess DNA-binding activity of dbUBF.
  • Site-directed mutagenesis of hydrophobic residues within the dimerization domain.

Related Experiment Videos

Main Results:

  • Recombinant dbUBF forms homodimers in vitro and binds nonselectively to double-stranded DNA.
  • Gel retardation assays showed multiple complexes formed by dbUBF dimers and DNA.
  • Mutagenesis of hydrophobic residues in the dimerization domain disrupted dbUBF association and altered DNA binding patterns.
  • Hydrophobic interactions within helical structures of the dimerization domain are critical for UBF association.

Conclusions:

  • UBF homodimerization is primarily driven by hydrophobic interactions between helices in the dimerization domain.
  • These hydrophobic interactions are essential for the formation of functional UBF dimers that interact with DNA.