Identification of nuclear type II [(3)H]estradiol binding sites as histone H4 |
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Authors: | Shoulars Kevin Brown Trellis Alejandro Mary Ann Crowley Jan Markaverich Barry M |
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Institution: | Department of Molecular and Cellular Biology and Center for Comparative Medicine, Baylor College of Medicine, One Baylor Plaza, 77030, Houston, TX, USA. |
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Abstract: | 3H]Luteolin binds covalently to uterine nuclear type II sites B. Markaverich, K. Shoulars, M.A. Alejandro, T. Brown, Steroids 66 (2001) 707] and was used to identify this protein(s). SDS-PAGE analyses of 3H]luteolin-labeled type II site preparations revealed specific binding to 11- and 35-kDa proteins. The 11-kDa protein was identified as histone H4 by amino acid sequencing. Western blotting confirmed that the 11- and 35-kDa proteins were acetylated forms of histone H4. Anti-histone H4 antibodies (but not H2A, H2B, or H3 antibodies) quantitatively immunoadsorbed type II binding sites from nuclear extracts. Binding analyses by 3H]estradiol exchange, using luteolin as a competitor, detected specific type II binding activity to histone H4 (but not histones H2A, H2B, or H3) generated in a rabbit reticulocyte lysate translation system and confirmed that histone H4 is the type II site. |
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Keywords: | Type II [3H]estradiol binding site Histone H4 Luteolin Bioflavonoid Methyl p-hydroxyphenyllactate (MeHPLA) Rat uterus |
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