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Chromatin condensation modulates access and binding of nuclear proteins.

Martin, Robert M. and Cardoso, M Cristina (2010):
Chromatin condensation modulates access and binding of nuclear proteins.
24(4), In: The FASEB journal : official publication of the Federation of American Societies for Experimental Biology, pp. 1066-1072, ISSN 1530-6860, [Online-Edition: http://www.cardoso-lab.org/publications/Martin_2009.pdf],
[Article]

Abstract

The condensation level of chromatin is controlled by epigenetic modifications and associated regulatory factors and changes throughout differentiation and cell cycle progression. To test whether changes of chromatin condensation levels per se affect access and binding of proteins, we used a hypertonic cell treatment. This shift to hyperosmolar medium increased nuclear calcium concentrations and induced a reversible chromatin condensation comparable to the levels in mitosis. However, this condensation was independent of mitotic histone H3 serine 10 phosphorylation. Photobleaching and photoactivation experiments with chromatin proteins-histone H2B-GFP and GFP-HP1alpha-before and after induced chromatin condensation demonstrated that hypercondensation reduced their dissociation rate and stabilized their chromatin binding. Finally, measuring the distribution of nucleoplasmic proteins in the size range from 30 to 230 kDa, we found that even relatively small proteins like GFP were excluded from highly condensed chromatin in living cells. These results suggest that structural changes in condensed chromatin by themselves affect chromatin access and binding of chromatin proteins independent of regulatory histone modifications.-Martin, R. M., Cardoso, M. C. Chromatin condensation modulates access and binding of nuclear proteins.

Item Type: Article
Erschienen: 2010
Creators: Martin, Robert M. and Cardoso, M Cristina
Title: Chromatin condensation modulates access and binding of nuclear proteins.
Language: English
Abstract:

The condensation level of chromatin is controlled by epigenetic modifications and associated regulatory factors and changes throughout differentiation and cell cycle progression. To test whether changes of chromatin condensation levels per se affect access and binding of proteins, we used a hypertonic cell treatment. This shift to hyperosmolar medium increased nuclear calcium concentrations and induced a reversible chromatin condensation comparable to the levels in mitosis. However, this condensation was independent of mitotic histone H3 serine 10 phosphorylation. Photobleaching and photoactivation experiments with chromatin proteins-histone H2B-GFP and GFP-HP1alpha-before and after induced chromatin condensation demonstrated that hypercondensation reduced their dissociation rate and stabilized their chromatin binding. Finally, measuring the distribution of nucleoplasmic proteins in the size range from 30 to 230 kDa, we found that even relatively small proteins like GFP were excluded from highly condensed chromatin in living cells. These results suggest that structural changes in condensed chromatin by themselves affect chromatin access and binding of chromatin proteins independent of regulatory histone modifications.-Martin, R. M., Cardoso, M. C. Chromatin condensation modulates access and binding of nuclear proteins.

Journal or Publication Title: The FASEB journal : official publication of the Federation of American Societies for Experimental Biology
Volume: 24(4)
Divisions: 10 Department of Biology > Cell Biology and Epigenetics
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10 Department of Biology
Date Deposited: 06 Mar 2010 16:23
Official URL: http://www.cardoso-lab.org/publications/Martin_2009.pdf
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