High-affinity binding site for a specific nuclear protein in the human IgM gene

Lothar Hennighausen, Ulrich Siebenlist, David Danner, Philip Leder, Dan Rawlins, Philip Rosenfeld, Thomas Kelly

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Proteins binding to specific regions of DNA with high affinity frequently govern or regulate reactions at the gene level. 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 cells and required for the in vitro replication of adenovirus (Ad) DNA. 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 repeat and the human c-myc gene. Although this site differs from the enhancer region, 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.

Original languageEnglish (US)
Pages (from-to)289-292
Number of pages4
Issue number6008
StatePublished - Dec 1 1985
Externally publishedYes


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Hennighausen, L., Siebenlist, U., Danner, D., Leder, P., Rawlins, D., Rosenfeld, P., & Kelly, T. (1985). High-affinity binding site for a specific nuclear protein in the human IgM gene. Nature, 314(6008), 289-292. https://doi.org/10.1038/314289a0