Isolation and Functional Analysis of the Promoter of the Bovine Serum Albumin Gene
Autor: | S. Cereghini, S.C. Power, Frank Gannon, A. Rollier |
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Rok vydání: | 1994 |
Předmět: |
Transcription
Genetic TATA box Molecular Sequence Data Biophysics Biology Transfection Polymerase Chain Reaction Biochemistry Cell Line Mice Liver Neoplasms Experimental Sequence Homology Nucleic Acid Tumor Cells Cultured Animals Deoxyribonuclease I Humans Protein–DNA interaction Binding site Bovine serum albumin Promoter Regions Genetic Molecular Biology Gene DNA Primers Sequence Deletion Cell Nucleus Base Sequence Cell Differentiation Serum Albumin Bovine Promoter Cell Biology Molecular biology Rats genomic DNA biology.protein Cattle |
Zdroj: | Biochemical and Biophysical Research Communications. 203:1447-1456 |
ISSN: | 0006-291X |
Popis: | The bovine serum albumin (bSA) promoter has been cloned from bovine genomic DNA using the polymerase chain reaction. In common with other albumin promoters, this promoter functions efficiently in the differentiated rat hepatoma cell line H4II and not in the its dedifferentiated derivative, H5. Analysis of 5' deletions of the bSA promoter after transient transfection into H4II has revealed that a short construct containing the HNF1 binding site and TATA box functions efficiently but requires the presence of the more upstream sequences to achieve full activity Footprint analysis of the promoter reveals seven sites of DNA protein interaction extending from -31 to -213. One of these sites, extending from -170 to -236, whose deletion results in a four fold increase in promoter activity. This site has not previously been reported in other albumin promoters and is bound by the C/EBP-like family of proteins. |
Databáze: | OpenAIRE |
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