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. 1989 Aug;9(8):3548–3552. doi: 10.1128/mcb.9.8.3548

Alteration of a single nucleotide allows efficient binding of H2TF1/KBF1 to the immunoglobulin kappa enhancer B motif.

F Mauxion 1, R Sen 1
PMCID: PMC362404  PMID: 2677676

Abstract

NF-kappa B (a protein present constitutively only in B cells) and H2TF1/KBF1 (a more ubiquitously distributed protein[s]) are two transcription factors that recognize very similar DNA sequences. However, the binding site associated with the kappa immunoglobulin gene enhancer (kappa B) is recognized predominantly by NF-kappa B. Using synthetically altered recognition sequences, we showed that the B-cell-specific NF-kappa B-binding site in the kappa enhancer can be converted to one that binds both NF-kappa B and the ubiquitous protein(s) H2TF1/KBF1 by substitution of a single nucleotide. Furthermore, transient transfection experiments suggested that NF-kappa B and H2TF1/KBF1 are functionally different even though their DNA recognition specificities are very similar.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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