title: Characterisation of chicken erythroid nuclear proteins which bind to the nuclease hypersensitive regions upstream of the beta A- and beta H-globin genes.
abstract: Chicken erythrocyte sequence-specific nuclear DNA-binding proteins, which bind to the 5'-flanking DNAseI hypersensitive sites of the erythrocyte chromosomal beta A- and beta H-globin genes, have been fractionated by HPLC gel filtration. Three beta A-globin gene DNA binding activities (to sites A, B and B' (10-12)) were separated. The erythroid precursor cell line HD3 has beta A-globin gene sites B and B' binding activities, but binding to site A is detected only after the HD3 cells are induced to differentiate. The fractionated protein binds to a redefined site B', which contains at its center the globin CACCC consensus sequence. The chromosomal beta H-globin gene has two 5'-flanking DNAseI hypersensitive sites which bracket two sequences (H and H') bound by erythrocyte and HD3 nuclear protein in vitro. The beta H- and beta A-globin gene binding sites (H and B) contain variants of the sequences bound by Nuclear Factor 1 and the TGGCA-binding protein, and their protein binding activity(ies) co-purify after HPLC gel filtration.
mesh_terms: D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D002645:Chickens; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004268:DNA-Binding Proteins / Q000032:analysis* / Q000302:isolation & purification; D003850:Deoxyribonuclease I / Q000494:pharmacology; D004912:Erythrocytes / Q000032:analysis*; D005786:Gene Expression Regulation; D005914:Globins / Q000235:genetics*; D008970:Molecular Weight; D009698:Nucleoproteins / Q000032:analysis* / Q000302:isolation & purification
chemical_list: D004268:DNA-Binding Proteins; D009698:Nucleoproteins; D005914:Globins; D003850:Deoxyribonuclease I