PMID: 8954154Nov 15, 1996Paper

Selective interaction between parathymosin and histone H1

European Journal of Biochemistry
K KondiliT Papamarcaki

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.

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Citations

Jul 23, 2002·Journal of Immunological Methods·Elena A SukhachevaAndrey B Vartapetian
Dec 4, 2001·Biochimica Et Biophysica Acta·V KoutrafouriG P Evangelatos
Jun 12, 2002·Molecular Biology of the Cell·Michael L WhitfieldDavid Botstein
Jul 21, 2000·European Journal of Biochemistry·N V ChichkovaA B Vartapetian
Aug 17, 2016·Molecular and Cellular Biology·Mitsuru OkuwakiKyosuke Nagata
Feb 18, 2005·The Journal of Biological Chemistry·Goran MarticThomais Papamarcaki
Jul 21, 2020·Epigenetics : Official Journal of the DNA Methylation Society·Nandini Karthik, Reshma Taneja
Oct 23, 2020·Life Science Alliance·Bin YuDongsheng Cai

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