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The Journal of Immunology, 2001, 166: 6704-6710.
Copyright © 2001 by The American Association of Immunologists

Dissociation of Pax-5 from KI and KII Sites During {kappa}-Chain Gene Rearrangement Correlates with Its Association with the Underphosphorylated Form of Retinoblastoma1

Hiromu Sato, Dan Wang and Akira Kudo2

Department of Life Science, Tokyo Institute of Technology, Yokohama, Japan

The KI and KII sites play a crucial role in {kappa}-chain gene rearrangement, which was investigated in mice deficient for these sites. Previously, we found that Pax-5 can bind to the KI and KII sites; however, the function of Pax-5 in {kappa}-chain gene rearrangement has not been investigated. Here, we have used an in vitro culture system in which differentiation from pre-B cells to immature B cells is induced by removing IL-7. We showed that, after the induction of differentiation, Pax-5 dissociated from the KI and KII revealed by EMSA analyses, and this dissociation occurred specifically at the KI and KII sites, but not at the Pax-5 binding site, in the CD19 promoter because of a lower binding affinity of Pax-5 for the KI and KII sites. During differentiation induced by removing IL-7, the underphosphorylated form of retinoblastoma preferentially associated with Pax-5, which caused dissociation of Pax-5 from KI and KII sites. These results suggest that the dissociation of Pax-5 from the KI and KII sites is important in the induction of {kappa}-chain gene rearrangement.




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