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Interaction of TAFII105 with Selected p65/RelA Dimers Is Associated with Activation of Subset of NF-κB Genes*

A. Yamit-hezi,S. Nir,O. Wolstein,R. Dikstein

Published 2000 in Journal of Biological Chemistry

ABSTRACT

TAFII105, a substoichiometric coactivator subunit of TFIID, is important for activation of anti-apoptotic genes by NF-κB in response to the cytokine tumor necrosis factor (TNF)-α. In the present study we have analyzed the mechanism of TAFII105 function with respect to its regulation of p65/RelA, a component of NF-κB. We found two independent p65/RelA-binding domains within the N terminus of TAFII105. One of these domains appears to be crucial for TAFII105-mediated anti-apoptotic gene activation in response to TNF-α. Analysis of the interaction between TAFII105 and different NF-κB complexes has revealed substantial differences in the affinity of TAFII105 toward different p65/RelA-containing dimers. We have identified the TNF-α induced anti-apoptotic A20 gene as a target gene of TAFII105. A20 has a differential protective effect on cell death induced by TNF-α in the presence of either the dominant negative mutant of TAFII105 (TAFII105ΔC) or the superdominant IκBα. The results suggest that the inhibitory effect of TAFII105ΔC on NF-κB-dependent genes is restricted to a subset of anti-apoptotic genes while the effect of IκBα is more general. Thus, an interaction between NF-κB and a specific coactivator is important for specifying target gene activation.

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