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Degradation of Promoter-bound p65/RelA Is Essential for the Prompt Termination of the Nuclear Factor B Response

¹ Institute for Research in Biomedicine, 6500 Bellinzona, Switzerland
² Department of Biological Sciences, Columbia University, New York, NY 10027

Address correspondence to Gioacchino Natoli, Institute for Research in Biomedicine, Via Vela 6, 6500 Bellinzona, Switzerland. Phone: 41-91-8200-318; Fax: 41-91-8200-305; email: gioacchino.natoli{at}irb.unisi.ch

Transcription factors of the nuclear factor (NF)-B/Rel family translocate into the nucleus upon degradation of the IBs. Postinduction repression of NF-B activity depends on NF-B–regulated resynthesis of IB, which dissociates NF-B from DNA and exports it to the cytosol. We found that after activation, p65/RelA is degraded by the proteasome in the nucleus and in a DNA binding–dependent manner. If proteasome activity is blocked, NF-B is not promptly removed from some target genes in spite of IB resynthesis and sustained transcription occurs. These results indicate that proteasomal degradation of p65/RelA does not merely regulate its stability and abundance, but also actively promotes transcriptional termination.

Key Words: NF-B • Rel family • proteasome • transcriptional regulation

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