Previous studies have shown that prothymosin a (ProT alpha) is a nucle
ar acidic protein implicated in cell proliferation. To identify protei
ns 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 ce
ntral acidic domain of ProT alpha, strongly inhibits the above interac
tion, suggesting that the binding of ProT alpha to histone H1 is media
ted through its acidic domain.