Nucleic Acids Research, 1986, Vol. 14, No. 19 7675-7693
© 1986
Articles |
Characterisation of chicken erythroid nuclear proteins which bind to the nuclease hypersensitive regions upstream of the ßA- and ß H-globin genes
Institute of Cancer Research: Royal Cancer Hospital, Chester Beatty Laboratories Fulham Road, London SW 3 6JB, UK
Received March 31, 1986. Accepted August 28, 1986.
Chicken erythrocyte sequence-specific nuclear DMA-binding proteins, which bind to the 5'-Flanking DNAsel hypersensitive sites of the erythrocyte chromosomal ßA- and ßH-globin genes, have been fractionated by HPLC gel filtration. Three ßA-globin gene DNA binding activities (to sites A, B and B' (10–12)) were separated. The erythroid precursor cell line HD3 has ßA-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 ßH-globin gene has two 5' -flanking DNAsel hypersensitive sites which bracket two sequences (H and H') bound by erythrocyte and HD3 nuclear protein in vitro. The ßH- and ßA-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.
+Present address: The Beatson Institute for Cancer Research, Switchback Road, Bearsden, Glasgow G61 1BD, UK
*Permanent address: All-Union Cancer Research Centre, 24 Kashirshoye Shosse, 115478 Moscow
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