A DNA-binding factor in adult hematopoietic cells interacts with a pyrimidine-rich domain upstream from the human delta-globin gene.

• DOI: 10.1073/pnas.88.20.8953
• Publication Date: 2006-05-31T11:47:54Z
• Authors: D O'Neill; K Bornschlegel; M Flamm; M Castle; A Bank
• Keywords: Nuclease

To date, DNA-binding factors with a developmental pattern of expression have not been described in human erythroid cells to explain the switch from fetal (gamma-) adult (delta- and beta-) globin gene expression. Here we describe factor present nuclear extracts mouse hematopoietic that binds an oligopyrimidine repeat approximately 960 base pairs upstream delta-globin gene. The binding site for is within unusual 250-base-pair domain greater than 95% pyrimidines on one strand. This preferentially sensitive S1 nuclease supercoiled plasmids, indicating it can adopt alternative non-B-DNA conformation. A number S1-sensitive sites domain, including factor-binding site, sequence characteristics associated formation triple helix (H-DNA). position between beta-globin-like genes, its potential adopting secondary structure, restricted activity tissues suggest possible roles cell development hemoglobin switching.