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

Selective interaction between parathymosin and histone H1

K Kondili1, O Tsolas, T Papamarcaki

  • 1Laboratory of Biological Chemistry, University of Ioannina, Medical School, Greece.

European Journal of Biochemistry
|November 15, 1996
PubMed
Summary

Parathymosin, an acidic nuclear protein, specifically binds to histone H1. This interaction, influenced by zinc ions and mediated by parathymosin's acidic domain, suggests a role in regulating histone H1 function.

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

On the intracellular trafficking of mouse S5 ribosomal protein from cytoplasm to nucleoli.

Journal of molecular biology·2009
Same author

Evaluation of five methods for determining low-density lipoprotein cholesterol (LDL-C) in hemodialysis patients(1).

Clinical biochemistry·2002
Same author

Routine differential diagnosis of proteinurias by capillary electrophoresis.

Clinical chemistry and laboratory medicine·2001
Same author

Partially reversible renal tubular damage in patients with obstructive jaundice.

Hepatology (Baltimore, Md.)·2001
Same author

Estimation of LDL cholesterol based on the Friedewald formula and on apo B levels.

Clinical biochemistry·2000
Same author

Nuclear distribution of prothymosin alpha and parathymosin: evidence that prothymosin alpha is associated with RNA synthesis processing and parathymosin with early DNA replication.

Experimental cell research·2000

Area of Science:

  • Molecular biology
  • Cell biology
  • Biochemistry

Background:

  • Parathymosin is an acidic polypeptide found in various tissues.
  • Its molecular interactions and functions remain incompletely understood.
  • Histone H1 is a crucial linker histone involved in chromatin structure and gene regulation.

Purpose of the Study:

  • To investigate the molecular associations of parathymosin.
  • To identify proteins that interact with parathymosin.
  • To elucidate the functional implications of parathymosin-histone H1 interactions.

Main Methods:

  • Ligand blotting assays were employed to screen for binding partners.
  • Native electrophoresis was used to study protein interactions under physiological conditions.

Related Experiment Videos

  • Immunoprecipitation confirmed specific molecular associations.

    • Main Results:

    • Parathymosin specifically binds to linker histone H1.
    • Zinc ions (Zn2+) enhance parathymosin-histone H1 binding.
    • Poly(glutamic acid) competed with parathymosin, indicating the acidic domain mediates binding.
    • Parathymosin interacts with the globular domain of histone H1.

    Conclusions:

    • Parathymosin forms a specific complex with histone H1.
    • The interaction is dependent on parathymosin concentration and influenced by Zn2+.
    • Parathymosin may function as a nuclear acidic protein modulating histone H1 activity.