Chromatin association and DNA binding properties of the c- fos proto-oncogene product (original) (raw)
Journal Article
European Molecular Biology Laboratory
Postfach 10.2209, D-6900 Heidelberg, FRG
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European Molecular Biology Laboratory
Postfach 10.2209, D-6900 Heidelberg, FRG
Search for other works by this author on:
European Molecular Biology Laboratory
Postfach 10.2209, D-6900 Heidelberg, FRG
Search for other works by this author on:
European Molecular Biology Laboratory
Postfach 10.2209, D-6900 Heidelberg, FRG
Search for other works by this author on:
Received:
17 October 1986
Revision received:
01 December 1986
Accepted:
01 December 1986
Published:
12 January 1987
PDF Cite
Manfred Renz, Bernard Verrier, Christina Kurz, Rolf Müller, Chromatin association and DNA binding properties of the c- fos proto-oncogene product , Nucleic Acids Research, Volume 15, Issue 1, 12 January 1987, Pages 277–292, https://doi.org/10.1093/nar/15.1.277
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Abstract
As a first step in the analysis of the molecular function of the nuclear c- fos proto-oncogene product we have studied its subnuclear localization in serum-stimulated mouse fibroblasts where it forms a non-covalent, apparently monodisperse complex with another nuclear protein, p39. The c- fos /p39 complex is almost quantitatively released from intact nuclei by DNasel or micrococcus nuclease treatment under conditions where only a minor fraction of DNA and nuclear proteins is released. In gel filtration experiments, c- fos /p39 comigrates with chromatin and seems to be associated with regions of increased DNasel accessibility. c- fos /p39 is bound to chromatin by electrostatic forces of moderate strength since >90% of the complex can be eluted from nuclei at 0.4 M NaCl. In vitro, the c- fos /p39 complex in nuclear extracts binds to double- and single-stranded calf thymus DNA, suggesting that the association of c- fos /p39 with chromatin is at least in part due to its interaction with DNA. In agreement with this conclusion, c- fos /p39 is released from nuclei by incubation with tRNA, presumably due to competition for binding sites. Our observations are compatible with the hypothesis that c- fos may play a role in the regulation of gene expression.
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