Prothymosin alpha associates with the oncoprotein SET and is involved in chromatin decondensation
Autor: | Karetsou, Z., Martic, G., Tavoulari, S., Christoforidis, S., Wilm, M., Gruss, C., Papamarcaki, T. |
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Jazyk: | angličtina |
Rok vydání: | 2004 |
Předmět: |
Cell Extracts
Male Silver Staining Chromosomal Proteins Non-Histone Blotting Western Molecular Sequence Data Proteins/chemistry/*metabolism Luciferases/metabolism Mass Spectrometry Protein Precursors/genetics/*metabolism Chromatin/*metabolism Sequence Analysis Protein Two-Hybrid System Techniques Humans Histone Chaperones Amino Acid Sequence Trans-Activators/metabolism Green Fluorescent Proteins/metabolism Nuclear Proteins/metabolism Recombinant Proteins/metabolism Spermatozoa/metabolism Plasmids/metabolism Thymosin/*analogs & derivatives/genetics/*metabolism CREB-Binding Protein Precipitin Tests Molecular Weight HeLa Cells Protein Binding Transcription Factors |
Popis: | Prothymosin alpha (ProTalpha) 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 ProTalpha forms a complex with the oncoprotein SET. ProTalpha efficiently decondenses human sperm chromatin, while overexpression of GFP-ProTalpha 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 ProTalpha function. FEBS Lett |
Databáze: | OpenAIRE |
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