A mutant Rel-homology domain promotes transcription by p50/NFκB1

Xiang Xu, Celine Gelinas

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

Previous studies showed that the binding of p50/NFκB1 to particular κB DNA sites altered its conformation in a way that correlated with transcriptional activation. Here, we investigated the effects of protein-protein interactions on the transcriptional activity of p50. We show that the association of p50 with a mutant Rel-homology domain (RHD) defective for DNA binding led to synergistic activation of κB site-dependent transcription, whereas neither protein alone had any effect. Partial proteolytic analysis showed that the conformation of p50 in these complexes differed from that in wild-type c-Rel-RHD/p50 complexes, and correlated with activated transcription. These results suggest that the Rel-homology domain can act as an allosteric effector to promote transcription by p50/NFκB1 and that the configuration of p50 is important for its activity. This also suggests that Rel proteins can promote transcription by other Rel-family members without binding to their DNA recognition site. These studies emphasize the important role of protein-protein interactions in Rel and NFκB-mediated transcription.

Original languageEnglish (US)
Pages (from-to)1521-1530
Number of pages10
JournalOncogene
Volume14
Issue number13
DOIs
StatePublished - Jan 1 1997

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All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics
  • Cancer Research

Keywords

  • C-Rel
  • NFκB
  • Protein conformation
  • Transcription
  • p50

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