Open Access Highly Accessed Research article

Functional characterization and gene expression profiling of Drosophila melanogaster short dADA2b isoform-containing dSAGA complexes

Tibor Pankotai1, Nóra Zsindely1, Edith E Vamos2, Orbán Komonyi1, László Bodai1 and Imre M Boros12*

Author affiliations

1 Department of Biochemistry and Molecular Biology, University of Szeged, Középfasor 52, H-6726, Szeged, Hungary

2 Institute of Biochemistry, Biological Research Center, Temesvári krt. 62, H-6726, Szeged, Hungary

For all author emails, please log on.

Citation and License

BMC Genomics 2013, 14:44  doi:10.1186/1471-2164-14-44

Published: 22 January 2013



ADA2 proteins, together with ADA3, SGF29 and GCN5 form the acetyltransferase module of GNAT-type histone acetyltransferase complexes. ADA2b is present in the SAGA complex, which plays roles in various chromatin-related processes via histone H3 modifications and by other mechanisms.


In this report we present findings showing that during Drosophila melanogaster development two dADA2b isoforms (dADA2bS and dADA2bL) - which differ in their C-terminal domains - are expressed at various levels. Genetic complementation experiments indicate that dADA2bS alone can support development but cannot fully complement dAda2b mutations. In the presence of dADA2bS, the SAGA-specific histone H3 acetylation level is partially restored in dAda2b mutants. Comparison of whole transcriptome profiles of dAda2b null and dAda2bS transgene-carrier dAda2b null larvae indicates partial overlap between affected genes. mRNA levels corresponding to selected genes which are either up- or down-regulated in dAda2b mutants are altered by dADA2bS expression to different extents, ranging from complete restoration to wild type levels to no restoration at all. The short (dADA2bS) isoform of dADA2b seems to be more capable of restoring lost dSAGA functions that cause mRNA level up-regulation than those that lead to decreased mRNA levels.


The data presented here are in accord with results of genetic complementation experiments, and support the hypothesis that different isoforms of dADA2b contribute to the functional variations of dSAGA multiprotein HAT complexes.

ADA2; SAGA complex; Histone acetylation; Microarray; GCN5