TFIIA Interacts with TFIID via Association with TATA-Binding Protein and TAF40

Abstract

TFIIA and TATA-binding protein (TBP) associate directly at the TATA element of genes transcribed by RNA polymerase II. In vivo, TBP is complexed with approximately 14 TBP-associated factors (TAFs) to form the general transcription factor TFIID. How TFIIA and TFIID communicate is not well understood. We show that in addition to making direct contacts with TBP, yeast TAF40 interacts directly and specifically with TFIIA. Mutational analyses of the Toa2 subunit of TFIIA indicate that loss of functional interaction between TFIIA and TAF40 results in conditional growth phenotypes and defects in transcription. These results demonstrate that the TFIIA-TAF40 interaction is important in vivo and indicate a functional role for TAF40 as a bridging factor between TFIIA and TFIID.

ACKNOWLEDGMENTS

This work was supported by NIH grant GM56884 to L.A.S.

We are indebted to Kevin Lumb for the Fos AD DNA and for critical reading of the manuscript. We also thank Zarmik Moqtaderi for various TAF DNAs.