Two different Drosophila ADA2 homologues are present in distinct GCN5 histone acetyltransferase-containing complexes

Selen Muratoglu, Sofia Georgieva, Gábor Pápai, Elisabeth Scheer, Izzet Enünlü, Orbán Komonyi, Imre Cserpán, Lubov Lebedeva, Elena Nabirochkina, A. Udvardy, László Tora, I. Boros

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Abstract

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 GCNS 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.

Original languageEnglish
Pages (from-to)306-321
Number of pages16
JournalMolecular and Cellular Biology
Volume23
Issue number1
DOIs
Publication statusPublished - Jan 2003

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Drosophila
TATA-Binding Protein Associated Factors
Drosophila Proteins
Polytene Chromosomes
Genes
Histone Acetyltransferases
Two-Hybrid System Techniques
Fungal Proteins
RNA Polymerase II
Alternative Splicing
X Chromosome
Glycerol
Transcriptional Activation
Gel Chromatography
Insects
human KAT2A protein
Proteins
Genome
Antibodies

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cell Biology

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Two different Drosophila ADA2 homologues are present in distinct GCN5 histone acetyltransferase-containing complexes. / Muratoglu, Selen; Georgieva, Sofia; Pápai, Gábor; Scheer, Elisabeth; Enünlü, Izzet; Komonyi, Orbán; Cserpán, Imre; Lebedeva, Lubov; Nabirochkina, Elena; Udvardy, A.; Tora, László; Boros, I.

In: Molecular and Cellular Biology, Vol. 23, No. 1, 01.2003, p. 306-321.

Research output: Contribution to journalArticle

Muratoglu, S, Georgieva, S, Pápai, G, Scheer, E, Enünlü, I, Komonyi, O, Cserpán, I, Lebedeva, L, Nabirochkina, E, Udvardy, A, Tora, L & Boros, I 2003, 'Two different Drosophila ADA2 homologues are present in distinct GCN5 histone acetyltransferase-containing complexes', Molecular and Cellular Biology, vol. 23, no. 1, pp. 306-321. https://doi.org/10.1128/MCB.23.1.306-321.2003
Muratoglu, Selen ; Georgieva, Sofia ; Pápai, Gábor ; Scheer, Elisabeth ; Enünlü, Izzet ; Komonyi, Orbán ; Cserpán, Imre ; Lebedeva, Lubov ; Nabirochkina, Elena ; Udvardy, A. ; Tora, László ; Boros, I. / Two different Drosophila ADA2 homologues are present in distinct GCN5 histone acetyltransferase-containing complexes. In: Molecular and Cellular Biology. 2003 ; Vol. 23, No. 1. pp. 306-321.
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abstract = "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 GCNS 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.",
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AU - Georgieva, Sofia

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AU - Scheer, Elisabeth

AU - Enünlü, Izzet

AU - Komonyi, Orbán

AU - Cserpán, Imre

AU - Lebedeva, Lubov

AU - Nabirochkina, Elena

AU - Udvardy, A.

AU - Tora, László

AU - Boros, I.

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AB - 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 GCNS 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.

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