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 HMG1 ta(i)le.

Alexander M Polyanichko1, Elena V Chikhirzhina, Alexei N Skvortsov

  • 1Molecular Biophysics Department, Physical Faculty of St.-Petersburg State University, 1 Ulianovskaya st., Stary Petergof, St.-Petersburg, 198904, Russia.

Journal of Biomolecular Structure & Dynamics
|May 25, 2002
PubMed
Summary

The C-terminal tail of High Mobility Group 1 (HMG1) protein significantly alters DNA structure. Removing this tail causes DNA to form highly ordered structures when bound by HMG1-domains.

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

E3 Ligases and Deubiquitinases in Controlling High-Mobility Group Box (HMGB) Protein Functions.

International journal of molecular sciences·2026
Same author

Modulation of Albumin Esterase Activity by Warfarin and Diazepam.

International journal of molecular sciences·2024
Same author

Rapid and selective colorimetric determination of L-DOPA in human serum with silver nanoparticles.

Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy·2023
Same author

Quantitative determination of albumin and immunoglobulin in human serum using gold nanoclusters.

Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy·2023
Same author

Structural Characteristics of High-Mobility Group Proteins HMGB1 and HMGB2 and Their Interaction with DNA.

International journal of molecular sciences·2023
Same author

tRNA as a stabilizing matrix for fluorescent silver clusters: photophysical properties and IR study.

Nanoscale advances·2022

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • High Mobility Group 1 (HMG1) protein is involved in DNA binding and structural modulation.
  • Understanding HMG1's interaction with DNA is crucial for elucidating its regulatory and architectural roles.
  • The influence of HMG1's distinct domains on DNA complex formation requires further investigation.

Purpose of the Study:

  • To investigate structural changes in DNA/protein complexes using circular dichroism (CD) spectroscopy.
  • To compare the DNA-binding behavior of HMG1 and a truncated variant (HMG1-(A+B)) lacking the C-terminal acidic tail.
  • To determine the role of the C-terminal tail in modulating HMG1-DNA interactions and complex structures.

Main Methods:

  • Circular dichroism (CD) spectroscopy was employed to analyze structural changes in DNA/protein complexes.

Related Experiment Videos

  • Studies were conducted using both purified calf thymus HMG1 protein and recombinant HMG1-(A+B) protein.
  • Experiments were performed at varying ionic strengths (15 mM NaCl and 150 mM NaCl) to assess differential binding.

    • Main Results:

    • At low ionic strength (15 mM NaCl), both HMG1 and HMG1-(A+B) exhibited similar interactions with calf thymus DNA.
    • At higher ionic strength (150 mM NaCl), HMG1-(A+B) binding to DNA resulted in distinct structural changes compared to HMG1.
    • HMG1-(A+B)/DNA complexes showed DNA fractions with very high optical activity, suggesting the formation of highly ordered DNA structures.

    Conclusions:

    • The negatively charged C-terminal acidic tail of HMG1 plays a critical role in modulating its interaction with DNA.
    • The absence of the C-terminal tail leads to the formation of highly ordered DNA structures, indicating a significant conformational change.
    • These findings highlight the functional importance of the HMG1 C-terminal tail and its domains in DNA binding and structural regulation.