Trichostatin A-induced histone acetylation causes decondensation of interphase chromatin
| Autor: | Monika Frank-Stöhr, Gabriele Müller, Michael Stöhr, Katalin Fejes Tóth, Christian P. Bacher, Tobias Knoch, Karsten Rippe, Malte Wachsmuth |
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| Rok vydání: | 2004 |
| Předmět: |
Chromosomal Proteins
Non-Histone Microscopy Energy-Filtering Transmission Electron Apoptosis Hydroxamic Acids Histone Deacetylases S Phase Histones Histone H2A Image Processing Computer-Assisted medicine Humans Nucleosome Interphase Cell Nucleus Protein Synthesis Inhibitors biology G1 Phase Acetylation Cell Biology Molecular biology Chromatin Genes cdc Fractals Histone Trichostatin A biology.protein Biophysics Histone deacetylase HeLa Cells medicine.drug |
| Zdroj: | Journal of Cell Science. 117:4277-4287 |
| ISSN: | 1477-9137 0021-9533 |
| DOI: | 10.1242/jcs.01293 |
| Popis: | The effect of trichostatin A (TSA)-induced histone acetylation on the interphase chromatin structure was visualized in vivo with a HeLa cell line stably expressing histone H2A, which was fused to enhanced yellow fluorescent protein. The globally increased histone acetylation caused a reversible decondensation of dense chromatin regions and led to a more homogeneous distribution. These structural changes were quantified by image correlation spectroscopy and by spatially resolved scaling analysis. The image analysis revealed that a chromatin reorganization on a length scale from 200 nm to >1 μm was induced consistent with the opening of condensed chromatin domains containing several Mb of DNA. The observed conformation changes could be assigned to the folding of chromatin during G1 phase by characterizing the effect of TSA on cell cycle progression and developing a protocol that allowed the identification of G1 phase cells on microscope coverslips. An analysis by flow cytometry showed that the addition of TSA led to a significant arrest of cells in S phase and induced apoptosis. The concentration dependence of both processes was studied. |
| Databáze: | OpenAIRE |
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