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Prothymosin α associates with the oncoprotein SET and is involved in chromatin decondensation
Author(s) -
Karetsou Zoe,
Martic Goran,
Tavoulari Sotiria,
Christoforidis Savvas,
Wilm Matthias,
Gruss Claudia,
Papamarcaki Thomais
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.09.091
Subject(s) - chromatin , microbiology and biotechnology , chromatin immunoprecipitation , coactivator , histone , chia pet , transcription (linguistics) , transcription factor , biology , chemistry , chromatin remodeling , promoter , genetics , gene , gene expression , linguistics , philosophy
Prothymosin α (ProTα) is a histone H1‐binding protein that interacts with the transcription coactivator CREB‐binding protein and potentiates transcription. Based on coimmunoprecipitation and mammalian two‐hybrid assays, we show here that ProTα forms a complex with the oncoprotein SET. ProTα efficiently decondenses human sperm chromatin, while overexpression of GFP–ProTα in mammalian cells results in global chromatin decondensation. These results indicate that decondensation of compacted chromatin fibers is an important step in the mechanism of ProTα function.