The Human TFIID Components TAFII135 and TAFII20 and the Yeast SAGA Components ADA1 and TAFII68 Heterodimerize to Form Histone-Like Pairs

doi:10.1128/MCB.20.1.340-351.2000

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Molecular and Cellular Biology, January 2000, p. 340-351, Vol. 20, No. 1
0270-7306/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

The Human TFIID Components TAF_II135 and TAF_II20 and the Yeast SAGA Components ADA1 and TAF_II68 Heterodimerize to Form Histone-Like Pairs

Yann-Gaël Gangloff, Sebastiaan Werten, Christophe Romier, Lucie Carré, Olivier Poch, Dino Moras, and Irwin Davidson^*

Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, Illkirch Cédex, C.U. de Strasbourg, France

Received 22 July 1999/Returned for modification 17 September 1999/Accepted 28 September 1999

It has been previously proposed that the transcription complexes TFIID and SAGA comprise a histone octamer-like substructureformed from a heterotetramer of H4-like human hTAF_II80 (or itsDrosophila melanogaster dTAF_II60 and yeast [Saccharomyces cerevisiae]yTAF_II60 homologues) and H3-like hTAF_II31 (dTAF_II40 and yTAF_II17)along with two homodimers of H2B-like hTAF_II20 (dTAF_II30 $alpha$ andyTAF_II61/68). However, it has not been formally shown that hTAF_II20heterodimerizes via its histone fold. By two-hybrid analysis withyeast and biochemical characterization of complexes formed bycoexpression in Escherichia coli, we showed that hTAF_II20 doesnot homodimerize but heterodimerizes with hTAF_II135. Heterodimerizationrequires the $alpha$ 2 and $alpha$ 3 helices of the hTAF_II20 histone fold andis abolished by mutations in the hydrophobic face of the hTAF_II20 $alpha$ 2 helix. Interaction with hTAF_II20 requires a domain of hTAF_II135which shows sequence homology to H2A. This domain also shows homologyto the yeast SAGA component ADA1, and we show that yADA1 heterodimerizeswith the histone fold region of yTAF_II61/68, the yeast hTAF_II20homologue. These results are indicative of a histone fold typeof interaction between hTAF_II20-hTAF_II135 and yTAF_II68-yADA1,which therefore constitute novel histone-like pairs in the TFIIDand SAGAcomplexes.

^* Corresponding author. Mailing address: Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP,B.P. 163-67404, Illkirch Cédex, C.U. de Strasbourg, France. Phone:33 3 88 65 34 40 (45). Fax: 33 3 88 65 32 01. E-mail: irwin{at}titus.u-strasbg.fr.

Molecular and Cellular Biology, January 2000, p. 340-351, Vol. 20, No. 1
0270-7306/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

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