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Trichostatin-A induces differential changes in histone protein dynamics and expression in HeLa cells

Journal Article · · Biochemical and Biophysical Research Communications
 [1];  [2]; ;  [3];  [3]
  1. SASTRA University, Tanjore 613402 (India)
  2. Raman Research Institute, Bangalore (India)
  3. National Centre for Biological Sciences, TIFR, Bellary Road, Bangalore 560065 (India)
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.
OSTI ID:
21032970
Journal Information:
Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 2 Vol. 363; ISSN BBRCA9; ISSN 0006-291X
Country of Publication:
United States
Language:
English

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