The Fos Protein Complex Is Associated with DNA in Isolated Nuclei and Binds to DNA Cellulose
- 12 December 1986
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 234 (4782) , 1417-1419
- https://doi.org/10.1126/science.3491427
Abstract
The properties of the viral and cellular fos proteins (Fos) were investigated as a first step toward understanding the function of the fos gene. Treatment of nuclei with salt and nonionic detergents solubilized a complex that contained Fos together with several other cellular proteins. The majority of the Fos protein complex was released from isolated nuclei incubated in the presence of deoxyribonuclease I or micrococcal nuclease but not with ribonuclease A, suggesting that Fos is associated with chromatin. This hypothesis is supported by the finding that Fos protein from native or denatured nuclear extracts exhibited DNA-binding activity in vitro. These results suggest that Fos is involved in the regulation of gene expression.Keywords
This publication has 24 references indexed in Scilit:
- The fos gene product undergoes extensive post-translational modification in eukaryotic but not in prokaryotic cellsGene, 1986
- Superinduction of c- fos by Nerve Growth Factor in the Presence of Peripherally Active BenzodiazepinesScience, 1985
- Induction of c-fos gene and protein by growth factors precedes activation of c-mycNature, 1984
- Platelet-derived growth factor induces rapid but transient expression of the c-fos gene and proteinNature, 1984
- Expression of the c- fos Gene and of an fos -Related Gene Is Stimulated by Platelet-Derived Growth FactorScience, 1984
- Stimulation of 3T3 cells induces transcription of the c-fos proto-oncogeneNature, 1984
- Viral and cellular fos proteins: A comparative analysisCell, 1984
- Nuclear location of the putative transforming protein of avian myelocytomatosis virusCell, 1982
- Thiol groups of liver alcohol dehydrogenase. Accessibility to general thiol reagents and to potential affinity‐labelsFEBS Letters, 1974
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970