The purification of a erythroid protein which binds to enhancer and promoter elements of haemoglobin genes

• Published in: Nucleic acids research Vol. 17; no. 4; pp. 1299 - 1314
• Main Authors: PERKINS, N. D, NICOLAS, R. H, PLUMB, M. A, GOODWIN, G. H
• Format: Journal Article
• Language: English
• Published: Oxford Oxford University Press 25.02.1989
• Subjects: Animals; Base Sequence; Binding Sites; Biological and medical sciences; Chickens; Chromatography, Affinity; Deoxyribonuclease I; Enhancer Elements, Genetic; Erythrocytes - metabolism; Fundamental and applied biological sciences. Psychology; Genes; Globins - genetics; hemoglobin; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Nuclear Proteins - blood; Promoter Regions, Genetic; promoters; Restriction Mapping; transcription factors; Transcription. Transcription factor. Splicing. Rna processing; Purification; Erythroid cell; Transcription promoter; Rodentia; Beta-Peptide chain; Molecular interaction; Binding site; Proteins; Vertebrata; Enhancer sequence; Mammalia; Gene; Mouse; Hemoglobin; Transcription factor
• ISSN: 0305-1048; 1362-4962
• DOI: 10.1093/nar/17.4.1299

An erythroid nuclear protein (EF1), originally detected as a protein binding within the nuclease hypersensitive site upstream of the chicken beta H-globin gene, has been purified. This protein of 37,000-39,000 molecular weight binds to three sites within the hypersensitive region: one between the CCAAT and TATA boxes, the second (further upstream) next to a NF1 binding site, and the third adjacent to a regulatory element found in a number of beta-globin genes. The EF1 protein also binds to an erythroid-specific promoter element of the mouse alpha-globin gene and to two sites within the chicken beta A-globin enhancer. These six EF1-binding sites are related by the consensus sequence A/TGATAA/GG/C. A minor protein of molecular weight 72,000 which co-purifies with EF1 also binds to the same sequences.