(Received for publication, March 19, 1996, and in revised form, May 24, 1996)

From the Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, Collège de France, B. P. 163, 67404 Illkirch Cédex, France

We have cloned and characterized the human TATA-binding protein (TBP)-associated factor hTAF_II55. hTAF_II55, which has no known Drosophila counterpart, is present in both of the previously described TFIID and TFIID subpopulations. We describe the interactions of hTAF_II55 with other subunits of the transcription factor TFIID. By cotransfection in COS cells, we show that hTAF_II55 interacts with hTAF_II250, hTAF_II100, hTAF_II28, hTAF_II20, and hTAF_II18, but not with hTAF_II30 or TBP. Analysis of the binding of hTAF_II55 and TBP to hTAF_II28 deletion mutants indicates that distinct regions of hTAF_II28 are required for these interactions. Although hTAF_II55 does not interact by itself with TBP, stable ternary complexes containing hTAF_II55 and TBP can be formed in the presence of hTAF_II250, hTAF_II100, or hTAF_II28. These results not only show that hTAF_II100 and hTAF_II28 interact with TBP, but also that they can nucleate the formation of partial TFIID complexes.

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