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

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10 Scopus citations


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 languageAmerican English
Pages (from-to)1521-1530
Number of pages10
Issue number13
StatePublished - 1997

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cancer Research


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

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