Interaction of DNA-binding proteins with the tissue-specific human apolipoprotein-AII enhancer

• Published in: Nucleic acids research Vol. 17; no. 6; pp. 2283 - 2300
• Main Authors: LUCERO, M. A, SANCHEZ, D, OCHOA, A. R, BRUNEL, F, COHEN, G. N, BARALLE, F. E, ZAKIN, M. M
• Format: Journal Article
• Language: English
• Published: Oxford Oxford University Press 25.03.1989
• Subjects: Apolipoprotein A-II; Apolipoproteins A - genetics; Base Sequence; Binding Sites; Biological and medical sciences; Cell Nucleus - analysis; Deoxyribonuclease I; DNA-Binding Proteins - metabolism; Enhancer Elements, Genetic; Fundamental and applied biological sciences. Psychology; HeLa Cells; Humans; Liver - ultrastructure; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Nuclear Proteins - metabolism; Regulatory Sequences, Nucleic Acid; Sequence Homology, Nucleic Acid; Transcription Factors - metabolism; Transcription. Transcription factor. Splicing. Rna processing; Human; Regulation(control); Enhancer sequence; Transcription; Liver; DNA binding protein; Molecular interaction; Binding site; Apolipoproteins; Transcription factor
• ISSN: 0305-1048; 1362-4962
• DOI: 10.1093/nar/17.6.2283

The identification of the binding sites for liver nuclear proteins present in the enhancer that control the cell specific transcription of the human apolipoprotein AII gene is reported. Five adjacent binding sites (motifs I to V) were identified. The motifs III, IV and V can be occupied differently by liver or HeLa nuclear proteins. Two hypersensitive zones (between motifs II-III and IV-V) are present only when liver nuclear extracts were tested. A first characterization of the factors reveal that motif IV interacts with the hepatic transcription factors Tf-LF1 (29) and LF-A1 (28, 30). A CCAAT binding protein, different from CTF/NF1, appears to bind to the motif II. The different binding sites share specific DNA sequences principally with 5' regulatory regions of other apolipoprotein genes.