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Molecular and Cellular Biology, January 2003, p. 306-321, Vol. 23, No. 1
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.1.306-321.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Two Different Drosophila ADA2 Homologues Are Present in Distinct GCN5 Histone Acetyltransferase-Containing Complexes

Selen Muratoglu,1,2,{dagger} Sofia Georgieva,3 Gábor Pápai,1 Elisabeth Scheer,2 Izzet Enünlü,1 Orbán Komonyi,4 Imre Cserpán,5 Lubov Lebedeva,3 Elena Nabirochkina,3 Andor Udvardy,1 László Tora,2 and Imre Boros1,4*

Institute of Biochemistry,1 Institute of Genetics,5 Biological Research Center, and Department of Genetics and Molecular Biology, University of Szeged, Szeged 6726, Hungary,4 Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, F-67404 Illkirch Cedex, CU de Strasbourg, France,2 Institute of Gene Biology, Russian Academy of Sciences, Moscow 117 334, Russia3

Received 8 July 2002/ Returned for modification 5 September 2002/ Accepted 1 October 2002

We have isolated a novel Drosophila (d) gene coding for two distinct proteins via alternative splicing: a homologue of the yeast adaptor protein ADA2, dADA2a, and a subunit of RNA polymerase II (Pol II), dRPB4. Moreover, we have identified another gene in the Drosophila genome encoding a second ADA2 homologue (dADA2b). The two dADA2 homologues, as well as many putative ADA2 homologues from different species, all contain, in addition to the ZZ and SANT domains, several evolutionarily conserved domains. The dada2a/rpb4 and dada2b genes are differentially expressed at various stages of Drosophila development. Both dADA2a and dADA2b interacted with the GCN5 histone acetyltransferase (HAT) in a yeast two-hybrid assay, and dADA2b, but not dADA2a, also interacted with Drosophila ADA3. Both dADA2s further potentiate transcriptional activation in insect and mammalian cells. Antibodies raised either against dADA2a or dADA2b both immunoprecipitated GCN5 as well as several Drosophila TATA binding protein-associated factors (TAFs). Moreover, following glycerol gradient sedimentation or chromatographic purification combined with gel filtration of Drosophila nuclear extracts, dADA2a and dGCN5 were detected in fractions with an apparent molecular mass of about 0.8 MDa whereas dADA2b was found in fractions corresponding to masses of at least 2 MDa, together with GCN5 and several Drosophila TAFs. Furthermore, in vivo the two dADA2 proteins showed different localizations on polytene X chromosomes. These results, taken together, suggest that the two Drosophila ADA2 homologues are present in distinct GCN5-containing HAT complexes.

* Corresponding author. Mailing address: Institute of Biochemistry, University of Szeged, Temesvari krt. 62, Szeged 6726, Hungary. Phone: 36 62 432 232 ext. 174. Fax: 36 62 433 506. E-mail: boros{at}nucleus.szbk.u-szeged.hu.

{dagger} Present address: Department of Pharmacology, George Washington University, Washington, DC 20037.

Molecular and Cellular Biology, January 2003, p. 306-321, Vol. 23, No. 1
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.1.306-321.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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