Prothymosin α binds to histone H1 in vitro
- 23 May 1994
- journal article
- Published by Wiley in FEBS Letters
- Vol. 345 (1), 71-75
- https://doi.org/10.1016/0014-5793(94)00439-0
Abstract
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.Keywords
This publication has 36 references indexed in Scilit:
- Chromatin as an essential part of the transcriptional mechanimNature, 1992
- Identification of a low-Mracidic nuclear protein as prothymosin αFEBS Letters, 1990
- Thymosins: both nuclear and cytoplasmic proteinsEuropean Journal of Biochemistry, 1990
- Histone H1 and the regulation of transcription of eukaryotic genesTrends in Biochemical Sciences, 1990
- Prothymosin α is an evolutionary conserved protein covalently linked to a small RNAFEBS Letters, 1989
- Prothymosin α is a nuclear proteinFEBS Letters, 1989
- Isolation and partial characterization of prothymosin α from porcine tissuesFEBS Letters, 1988
- Lamin B constitutes an intermediate filament attachment site at the nuclear envelope.The Journal of cell biology, 1987
- Salt-dependent co-operative interaction of histone H1 with linear DNAJournal of Molecular Biology, 1986
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970