Nucleic Acids Research, 1990, Vol. 18, No. 17 5119-5126
© 1990
MOLECULAR BIOLOGY |
Properties of BGP1, a poly(dG)-binding protein from chicken erythrocytes
Laboratory of Molecular Biology, National Institute of Diabetes, and Digestive and Kidney Diseases 9000 Rockville Pike, Bethesda, MD 20892, USA
*To whom correspondence should be addressed
Received May 31, 1990. Revised July 30, 1990. Accepted July 30, 1990.
The chicken ßA-globin gene contains in the neighborhood of its 5' promoter a (dG)-homopolymer sequence 16 base pairs long. The 66 kD protein BGP1 (beta globin protein 1), isolated from chicken erythrocytes, has been shown to bind specifically to this sequence (1). We describe further purification of BGP1, measure its affinity for the ßA-globin promoter binding site, and analyze its binding properties. The minimal binding sequence is seven dG residues; methylation interference studies show that each of these residues contacts BGP1. Binding competition experiments employing (dG)·(dC) oligomers of varying lengths also are consistent with (dG)7 as a minimum recognition sequence. All of the data can be explained by a model in which BGP1 binds to any contiguous set of seven (dG) residues, so that the effective constant for binding to (dG)n is proportional to n minus 6. This behavior may be typical of proteins that bind specifically to repeated sequences.
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