Nucleic Acids Research, 1989, Vol. 17, No. 22 9015-9026
© 1989
CHEMISTRY |
Purification and characterization of a protein that binds to the recombination signal sequence of the immunoglobulin Jx segment
Department of Medical Chemistiy, Kyoto University Faculty of Medicine Yoshida, Sakyo-ku, Kyoto 606, Japan
Received September 4, 1989. Revised October 23, 1989. Accepted October 23, 1989.
A protein that binds to the recombination signal sequence (RS) of the immunoglobulin Jx segment was purified almost to homogeneity from the nuclear extract of a murine pre-B cell line 38B9. A similar binding protein was found in lymphoid cell lines but not in non-lyrnphoid cell lines. The binding activity was associated with a polypeptide with a molecular weight of 60,000. DNase I footprinting analysis demonstrated that this binding protein interacted with the heptamer and several 3' bases close to the heptamer. The Kd value of the Jx RS binding protein to the Jx RS was 1 nM. One base substitution in the heptamer of the Jx RS greatly reduced the affinity of the Jx RS binding protein. The high specificity of the binding site of the Jx RS binding protein suggests that this protein may be involved in V-J recombination.
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