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Histone H1 and chromatin interactions in human fibroblast nuclei after H1 depletion and reconstitution with H1 subfractions
Linköping University, Faculty of Health Sciences. Linköping University, Department of Clinical and Experimental Medicine, Cell Biology.
2004 (English)In: Cytometry, ISSN 0196-4763, Vol. 58A, no 2, 132-139 p.Article in journal (Refereed) Published
Abstract [en]

Background: Linker histones constitute a family of lysine-rich proteins associated with nucleosome core particles and linker DNA in eukaryotic chromatin. In permeabilized cells, they can be extracted from nuclei by using salt concentration in the range of 0.3 to 0.7 M. Although other nuclear proteins are also extracted at 0.7 M salt, the remaining nucleus represents a template that is relatively intact. Methods: A cytochemical method was used to study the affinity of reconstituted linker histones for chromatin in situ in cultured human fibroblasts. We also investigated their ability to condense chromatin by using DNA-specific osmium ammine staining for electron microscopy. Results: Permeabilized and H1-depleted fibroblast nuclei were suitable for the study of linker histone-chromatin interactions after reconstitution with purified linker histone subfractions. Our results showed that exogenous linker histones bind to chromatin with lower affinity than the native ones. We detected no significant differences between the main H1 and H1degrees histone fractions with respect to their affinity for chromatin or in their ability to condense chromatin. Conclusions: Linker histone interactions with chromatin are controlled also by mechanisms independent of linker histone subtype composition. (C) 2004 Wiley-Liss, Inc.

Place, publisher, year, edition, pages
2004. Vol. 58A, no 2, 132-139 p.
Keyword [en]
chromatin, linker histones, binding, affinity, 4 ', 6-diamidino-2-phenylindole, image cytofluorometry
National Category
Medical and Health Sciences
URN: urn:nbn:se:liu:diva-46247DOI: 10.1002/cyto.a.10119OAI: diva2:267143
Available from: 2009-10-11 Created: 2009-10-11 Last updated: 2011-01-12

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Rundquist, Ingemar
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