Nucleoprotein complexes that regulate gene expression in adipocyte differentiation: direct participation of c- fos

• Published in: Cell Vol. 49; no. 6; pp. 835 - 844
• Main Authors: Distel, Robert J., Ro, Hyo-Sung, Rosen, Barry S., Groves, Douglas L., Spiegelman, Bruce M.
• Format: Journal Article
• Language: English
• Published: Cambridge, MA Elsevier Inc 19.06.1987; Cell Press
• Subjects: Adipose Tissue - physiology; Animals; Base Sequence; Biological and medical sciences; Carrier Proteins - genetics; Cell Differentiation; Chromosome Mapping; Complement Factor D; DNA-Binding Proteins - physiology; Endopeptidases - genetics; Fatty Acid-Binding Protein 7; Fatty Acid-Binding Proteins; Fundamental and applied biological sciences. Psychology; Gene expression; Gene Expression Regulation; Glycerolphosphate Dehydrogenase - genetics; Mice; Molecular and cellular biology; Molecular genetics; Neoplasm Proteins; Nerve Tissue Proteins; Nucleoproteins - physiology; Promoter Regions, Genetic; Proto-Oncogene Proteins - physiology; Proto-Oncogenes; Serine Endopeptidases; Transcription Factors - genetics; Transcription Factors - physiology; Proteins; Adipocyte; Regulation(control); Animal; DNA; C-Onc gene; Molecular interaction; Activation; Molecular complex; Cell differentiation; Gene expression
• ISSN: 0092-8674; 1097-4172
• DOI: 10.1016/0092-8674(87)90621-0

Adipocyte differentiation is accompanied by the transcriptional activation of many new genes, including a putative lipid-binding protein termed adipocyte P2 (aP2). The aP2 gene contains a regulatory element (FSE2) 124 bases 5′ to its start of transcription. This element binds nuclear factors in sequence-specific and differentiation-dependent fashion as determined by altered mobility in gel retardation assays. Deletion analysis of promoter-linked transfection assays and competition of these constructions in cells with a synthetic FSE2 element suggest that trans-acting factors bind to this region and act as negative regulators of aP2 gene activity in preadipocytes. c- fos appears to participate directly in this nucleoprotein complex, as demonstrated by the ability of antibodies to c- fos to disrupt specific binding of factors to the FSE2 sequence but not to factor-binding sequences from several other genes. Antibodies to c- fos specifically immunoprecipitate protein complexes covalently bound to FSE2 DNA via UV cross-linking.