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PMID: 2495523 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

Nucleic acids research ·Vol. 17 ·No. 6 ·1989-03-25 ·Pages 2283-300

Lucero MA, Sanchez D, Ochoa AR, Brunel F, Cohen GN, Baralle FE, Zakin MM

Abstract

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.

MeSH Terms
Apolipoprotein A-II Apolipoproteins A/genetics Base Sequence Binding Sites Cell Nucleus/analysis DNA-Binding Proteins/metabolism Deoxyribonuclease I Enhancer Elements, Genetic HeLa Cells Humans Liver/ultrastructure Molecular Sequence Data Nuclear Proteins/metabolism Regulatory Sequences, Nucleic Acid Sequence Homology, Nucleic Acid Transcription Factors/metabolism
Chemicals
Apolipoprotein A-II Apolipoproteins A DNA-Binding Proteins Nuclear Proteins Transcription Factors Deoxyribonuclease I
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Lucero M A
Unité de Biochimie Cellulaire, Institut Pasteur, Paris, France.
Sanchez D
Ochoa A R
Brunel F
Cohen G N
Baralle F E
Zakin M M
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
Published
1989-03-25
Pages
2283-300
Language
English
Region
England
NLM ID
0411011
PMCID
PMC317596
Subset
IM
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