Journal list menu

Volume 242, Issue 1 p. 67-74
Free Access

Selective Interaction Between Parathymosin and Histone H1

Katerina Kondili

Katerina Kondili

Laboratory of Biological Chemistry, University of Ioannina, Medical School, Ioannina, Greece

Search for more papers by this author
Orestes Tsolas

Orestes Tsolas

Laboratory of Biological Chemistry, University of Ioannina, Medical School, Ioannina, Greece

Search for more papers by this author
Thomais Papamarcaki

Corresponding Author

Thomais Papamarcaki

Laboratory of Biological Chemistry, University of Ioannina, Medical School, Ioannina, Greece

T. Papamarcaki, Laboratory of Biological Chemistry, University of Ioannina Medical School, 451 10 Ioannina, Greece
Fax:+30 651 33442Search for more papers by this author
First published: November 1996
Citations: 17

Abstract

We have studied the molecular associations of parathymosin, an acidic polypeptide with a wide tissue distribution, by means of three approaches; ligand blotting; native electrophoresis; and immunoprecipitation. We report here that parathymosin binds specifically to the linker histone H1. This binding is enhanced by Zn2+ and is dependent on the concentration of parathymosin. Poly(glutamic acid) is able to compete fully with parathymosin for binding to histone H1, suggesting that this interaction is mediated by the acidic domain of the protein. Moreover, we demonstrate that parathymosin interacts with the globular domain of histone H1 under native conditions. Based on these data, we postulate that parathymosin may belong to a group of nuclear acidic proteins that affect histone H1 function.

Abbreviations

  • FITC
  • fluorescein isothiocyanate
  • GH1
  • globular domain of histone H1
  • NLS
  • nuclear-localization signal
  • PhMeSO2F
  • phenylmethylsulfonyl fluoride
  • Enzymes

  •  
  • Phosphofructokinase 1 (EC 2.7.1.11)
  •  
  • trypsin (EC 3.4.21.4)
  •  
  • peroxidase (EC 1.11.17)