Abstract
Proteins binding to specific regions of DNA with high affinity frequently govern or regulate reactions at the gene level1–8. We have identified a high-affinity binding site in the immunoglobulin μ gene that binds a specific nuclear protein, and have now characterized it fully using nuclear factor 1 (NF-1), a protein purified from the nuclei of HeLa cells9,10 and required for the in vitro replication of adenovirus (Ad) DNA9–12. NF-1 protects a 25-base pair (bp) double-stranded segment of DNA which shares a consensus sequence, 5′ TGGA/CNNNNNGCCAA 3′, with similar binding sites in the Ad-5 terminal repeat10–12 and the human c-myc gene13. Although this site differs from the enhancer region13–16, a biological function is suggested by the fact that it is DNase I hypersensitive in immunoglobulin-producing lymphoblastoid cells. The binding site for the NF-1 protein in the μ gene, by analogy with the site in the Ad-5 terminal repeat, may represent one component of a cellular origin of replication; alternatively, it may be responsible for the activation of the chromatin in this region.
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Hennighausen, L., Siebenlist, U., Danner, D. et al. High-affinity binding site for a specific nuclear protein in the human IgM gene. Nature 314, 289–292 (1985). https://doi.org/10.1038/314289a0
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DOI: https://doi.org/10.1038/314289a0
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