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Molecular and Cellular Biology, August 2001, p. 5109-5121, Vol. 21, No. 15
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.15.5109-5121.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

The TFIID Components Human TAFII140 and Drosophila BIP2 (TAFII155) Are Novel Metazoan Homologues of Yeast TAFII47 Containing a Histone Fold and a PHD Finger

Yann-Gaël Gangloff,1 Jean-Christophe Pointud,2 Sylvie Thuault,1 Lucie Carré,1 Christophe Romier,1 Selen Muratoglu,3 Marjorie Brand,1 Laszlo Tora,1 Jean-Louis Couderc,2 and Irwin Davidson1,*

Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, 67404 Illkirch Cédex, C.U. de Strasbourg,1 and Institut National de la Santé et de la Recherche Médicale U384, Laboratoire de Biochimie, UFR Médecine, 63001 Clermont-Ferrand,2 France, and Institute of Biochemistry, Biological Research Center, Szeged 6701, Hungary3

Received 25 January 2001/Returned for modification 26 February 2001/Accepted 28 April 2001

The RNA polymerase II transcription factor TFIID comprises the TATA binding protein (TBP) and a set of TBP-associated factors (TAFIIs). TFIID has been extensively characterized for yeast, Drosophila, and humans, demonstrating a high degree of conservation of both the amino acid sequences of the constituent TAFIIs and overall molecular organization. In recent years, it has been assumed that all the metazoan TAFIIs have been identified, yet no metazoan homologues of yeast TAFII47 (yTAFII47) and yTAFII65 are known. Both of these yTAFIIs contain a histone fold domain (HFD) which selectively heterodimerizes with that of yTAFII25. We have cloned a novel mouse protein, TAFII140, containing an HFD and a plant homeodomain (PHD) finger, which we demonstrated by immunoprecipitation to be a mammalian TFIID component. TAFII140 shows extensive sequence similarity to Drosophila BIP2 (dBIP2) (dTAFII155), which we also show to be a component of Drosophila TFIID. These proteins are metazoan homologues of yTAFII47 as their HFDs selectively heterodimerize with dTAFII24 and human TAFII30, metazoan homologues of yTAFII25. We further show that yTAFII65 shares two domains with the Drosophila Prodos protein, a recently described potential dTAFII. These conserved domains are critical for yTAFII65 function in vivo. Our results therefore identify metazoan homologues of yTAFII47 and yTAFII65.

* Corresponding author. Mailing address: Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, BP 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, August 2001, p. 5109-5121, Vol. 21, No. 15
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.15.5109-5121.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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