Selective interaction between parathymosin and histone H1.
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.
Kondili
K
K
Laboratory of Biological Chemistry, University of Ioannina, Medical School, Greece.
Tsolas
O
O
Papamarcaki
T
T
D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones / Q000378:metabolism*; D006801:Humans; D008856:Microscopy, Fluorescence; D008969:Molecular Sequence Data; D013947:Thymosin / Q000031:analogs & derivatives* / Q000378:metabolism; D014407:Tumor Cells, Cultured; D015032:Zinc / Q000494:pharmacology
D006657:Histones; D013947:Thymosin; C044498:parathymosin alpha; D015032:Zinc