Prothymosin α binds to histone H1 in vitro

FEBS Letters

Tsolas, Orestes¹  Papamarcaki, Thomais¹ 

[1] Laboratory of Biological Chemistry, University of Ioannina Medical School, 451 10 Ioannina, Greece

关键词: Prothymosin α;    Thymosin αl;    Nucleosome;    Histone H1;    Ligand-blotting assay;    ECL;    enhanced chemiluminescence;    Pro Tα;    prothymosin α;    SDS-PAGE;    sodium dodecyl sulfate polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(94)00439-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Previous studies have shown that prothymosin α (Pro Tα) is a nuclear acidic protein implicated in cell proliferation. To identify proteins that interact with Pro Tα we have used ligand-blotting assays. We report here that purified Pro Tα binds specifically to histone H1 in a dose dependent manner. Polyglutamic acid, an analog of the central acidic domain of Pro Tα, strongly inhibits the above interaction, suggesting that the binding of Pro Tα to histone H1 is mediated through its acidic domain.

【 授权许可】

Unknown