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Nucleic Acids Research, 1989, Vol. 17, No. 4 1299-1314
© 1989

MOLECULAR BIOLOGY

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

Neil D. Perkins, Robert H. Nicolas, Mark A. Plumb1 and Graham H. Goodwin*

Institute of Cancer Research, Chester Beatty Laboratories Fulham Road, London SW3 6JB 1Beatson Institute for Cancer Research Glasgow, UK

*To whom correspondence should be addressed

Received December 2, 1988. Accepted January 17, 1989.

An erythroid nuclear protein (EF1), originally detected as a protein binding within the nuclease hypersensitive site upstream of the chicken ßH-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 ß-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 ßA 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.


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