PROTHYMOSIN-ALPHA BINDS TO HISTONE H1 IN-VITRO

被引：76

作者：

PAPAMARCAKI, T

TSOLAS, O

机构：

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

来源：

FEBS LETTERS | 1994年 / 345卷 / 01期

关键词：

PROTHYMOSIN ALPHA; THYMOSIN ALPHA-1; NUCLEOSOME; HISTONE H1; LIGAND-BLOTTING ASSAY;

D O I：

10.1016/0014-5793(94)00439-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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

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页码：71 / 75

页数：5

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