Novel sites in the p65 subunit of NF-kappa B interact with TFIIB to facilitate NF-kappa B induced transcription.
217 - 222.
Nuclear factor kappaB (NF-kappaB) transcription factors regulate a large number of genes in response to inflammation, infection and stressful conditions. In this study, we investigated whether NF-kappaB p65 regulates the transcription of target genes by interacting with components of the basal transcription machinery. We examined the interaction of p65 with the basal transcription factor IIB (TFIIB). Glutathione S-transferase pull down assays showed that the Rel homology domain of p65 is important for binding to TFIIB. Molecular modelling, together with the generation of specific point mutants, revealed that residues 41 R and 42 S in the Rel homology domain of p65 facilitate the interaction with TFIIB. Mutation of these residues showed a decrease in p65 induced transcription, suggesting that they are involved in a functional interaction with TFIIB. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
|Title:||Novel sites in the p65 subunit of NF-kappa B interact with TFIIB to facilitate NF-kappa B induced transcription|
|Keywords:||protein-protein interaction, nuclear factor kappa B, transcription factor IIB, transcriptional regulation, RNA-POLYMERASE-II, TRANSACTIVATION DOMAIN, FUNCTIONAL INTERACTION, CRYSTAL-STRUCTURE, TERMINAL DOMAIN, PROTEINS, RECEPTOR, COMPLEX, BINDING, PHOSPHORYLATION|
|UCL classification:||UCL > School of Life and Medical Sciences
UCL > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > School of Life and Medical Sciences > Faculty of Life Sciences > Biosciences (Division of) > Structural and Molecular Biology
UCL > School of Life and Medical Sciences > Faculty of Medical Sciences
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