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Molecular and Cellular Biology, March 2000, p. 1639-1648, Vol. 20, No. 5
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Two Novel Drosophila TAFIIs Have Homology with Human TAFII30 and Are Differentially Regulated during Development

Sofia Georgieva,1,2,3 Doris B. Kirschner,1 Tereza Jagla,4 Elena Nabirochkina,2,3 Susanne Hanke,5 Heide Schenkel,5 Cécilia de Lorenzo,5 Pradip Sinha,6 Krysztof Jagla,4 Bernard Mechler,5 and Làszlò Tora1,*

Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, F-67404 Illkirch Cedex, CU de Strasbourg,1 and INSERM U.384, 63001 Clermont Ferrand Cedex,4 France; Institute of Gene Biology, Russian Academy of Sciences,2 and University of Oslo, Center of Medical Studies,3 Moscow, Russia; Department of Development Genetics, Deutsches Krebsforschungszentrum, D-69120 Heidelberg, Germany5; and Drosophila Stock Center, School of Life Sciences, Devi Ahilya, Vishwavidyala, Vigyan Bhawan, Indore 452-001, India6

Received 26 July 1999/Returned for modification 31 August 1999/Accepted 18 November 1999

TFIID is a multiprotein complex composed of the TATA binding protein (TBP) and TBP-associated factors (TAFIIs). The binding of TFIID to the promoter is the first step of RNA polymerase II preinitiation complex assembly on protein-coding genes. Yeast (y) and human (h) TFIID complexes contain 10 to 13 TAFIIs. Biochemical studies suggested that the Drosophila (d) TFIID complexes contain only eight TAFIIs, leaving a number of yeast and human TAFIIs (e.g., hTAFII55, hTAFII30, and hTAFII18) without known Drosophila homologues. We demonstrate that Drosophila has not one but two hTAFII30 homologues, dTAFII16 and dTAFII24, which are encoded by two adjacent genes. These two genes are localized in a head-to-head orientation, and their 5' extremities overlap. We show that these novel dTAFIIs are expressed and that they are both associated with TBP and other bona fide dTAFIIs in dTFIID complexes. dTAFII24, but not dTAFII16, was also found to be associated with the histone acetyltransferase (HAT) dGCN5. Thus, dTAFII16 and dTAFII24 are functional homologues of hTAFII30, and this is the first demonstration that a TAFII-GCN5-HAT complex exists in Drosophila. The two dTAFIIs are differentially expressed during embryogenesis and can be detected in both nuclei and cytoplasm of the cells. These results together indicate that dTAFII16 and dTAFII24 may have similar but not identical functions.

* Corresponding author. Mailing address: Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, BP 163, F67404 Illkirch Cedex, CU de Strasbourg, France. Phone: 33 388 65 34 44. Fax: 33 388 65 32 01. E-mail: laszlo{at}igbmc.u-strasbg.fr.

Molecular and Cellular Biology, March 2000, p. 1639-1648, Vol. 20, No. 5
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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