Trichostatin-A induces differential changes in histone protein dynamics and expression in HeLa cells
Autor: | Apurva Sarin, Dipanjan Bhattacharya, G. V. Shivashankar, Jyothsna Rao, Bidisha Banerjee |
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Rok vydání: | 2007 |
Předmět: |
Biophysics
Biology Hydroxamic Acids Biochemistry Histone Deacetylases Chromatin remodeling Histones Histone H1 Histone H2A medicine Humans Histone code Histone octamer Phosphorylation Molecular Biology Dose-Response Relationship Drug Acetylation Cell Biology Chromatin Cell biology Histone Deacetylase Inhibitors Trichostatin A Gene Expression Regulation sense organs Histone deacetylase HeLa Cells medicine.drug |
Zdroj: | Biochemical and Biophysical Research Communications. 363:263-268 |
ISSN: | 0006-291X |
DOI: | 10.1016/j.bbrc.2007.08.120 |
Popis: | Trichostatin-A (TSA), a histone deacetylase (HDAC) inhibitor, results in enhanced acetylation of core histones thereby disrupting chromatin organization within living cells. We report on changes in chromatin organization and the resultant alteration in nuclear architecture following treatment with TSA using fluorescence imaging. TSA triggers an expected increase in the euchromatin fraction which is accompanied by a significant increase in nuclear volume and alterations in chromatin compaction mapped using fluorescence anisotropy imaging. We observe differential changes in the mobility of core and linker histones as measured by fluorescence recovery after photo-bleaching (FRAP) and fluorescence correlation spectroscopy (FCS) methods. Further TSA induces a differential increase in linker histone transcription and increased phosphorylation of linker histone proteins accompanying an expected increase in core histone acetylation patterns. Thus subtle feedback responses triggered by changes in chromatin configurations impinge selectively on linker histone mobility and its expression. These observations have implications for understanding the role of HDAC in the dynamic maintenance of chromatin organization. |
Databáze: | OpenAIRE |
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