Prothymosin α associates with the oncoprotein SET and is involved in chromatin decondensation

Autor:	Thomais Papamarcaki, Sotiria Tavoulari, Zoe Karetsou, Savvas Christoforidis, Claudia Gruss, Goran Martic, Matthias Wilm
Jazyk:	angličtina
Předmět:	Cell Extracts Male Chromosomal Proteins Non-Histone Prothymosin Alpha Biochemistry Oncoprotein SET Mass Spectrometry Sequence Analysis Protein Structural Biology Transcription (biology) Luciferases Chromatin decondensation CREB-binding protein Nuclear Proteins Spermatozoa Chromatin Recombinant Proteins Cell biology DNA-Binding Proteins Histone Plasmids Protein Binding Silver Staining Immunoprecipitation Blotting Western Green Fluorescent Proteins Molecular Sequence Data Biophysics Biology Two-Hybrid System Techniques Genetics Humans Histone Chaperones Amino Acid Sequence Protein Precursors Molecular Biology Transcription factor Proteins Prothymosin α Cell Biology Precipitin Tests Molecular biology Molecular Weight Thymosin Transcription Coactivator Trans-Activators biology.protein HeLa Cells Transcription Factors
Zdroj:	FEBS Letters. (3):496-500
ISSN:	0014-5793
DOI:	10.1016/j.febslet.2004.09.091
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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1214b8627c13eb31bd833aef09c1094 Zobrazit plný text záznamu