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Nucleic Acids Research, 1988, Vol. 16, No. 11 4967-4988
© 1988

Articles

Identification and partial purification of a protein binding to the human immunoglobulin kappa enhancer xE2 site

Jeffrey M. Gimble{dagger}, James R. Flanagan, David Recker and Edward E. Max*

Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, National Institutes of Health Building 5 Room B1-04, Bethesda, MD 20892, USA

*To whom correspondence should be addressed

Received December 17, 1987. Revised April 20, 1988. Accepted April 20, 1988.

We previously described a domain in the 5' half of the human immunoglobulin {kappa} enhancer which could bind nuclear proteins in vitro, as detected by a {lambda} exonuclease protection assay. A second more 3' binding domain in the enhancer has now been detected by a similar assay employing a different exonuclease, the T7 gene 6 exonuclease. Using this assay and starting with a pig spleen nuclear extract, we have purified 5000-fold a protein that binds to the 3' domain. In a DNase I footprint experiment the partially purified protein protects a 27 bp segment in the enhancer centered around the sequence CAGGTGGC, which corresponds to the {kappa}E2 sequence motif described in the mouse {kappa} enhancer. The protein, designated NF-{kappa}E2, also appears to bind at a position downstream of {kappa}E2, at or near the {kappa}E3 site. Proteins capable of binding at {kappa}E2 are found in several mammalian species and are expressed in both lymphoid and non-lymphoid tissues.

{dagger}Present address: Oklahoma Medical Research Foundation, Immunobiology and Cancer Division, 825 N.E. 13th Street, Oklahoma City, OK 73104, USA


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