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Two Drosophila Ada2 homologues function in different multiprotein complexes.

Thomas Kusch1, Sebastián Guelman, Susan M Abmayr

  • 1Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.

Molecular and Cellular Biology
|April 17, 2003
PubMed
Summary
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Drosophila possess two Ada2 variants, dAda2a and dAda2b, impacting gene regulation. Only dAda2b is part of SAGA complexes, while dAda2a associates with Gcn5 independently, suggesting novel transcriptional roles.

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Gene Regulation

Background:

  • Histone acetylation is vital for DNA processes like transcription, repair, and replication.
  • Gcn5-containing N-acetyltransferase (GNAT) complexes catalyze histone acetylation.
  • Conserved subunits like Ada2, Ada3, Spt3, and Tra1/TRRAP are found in GNAT complexes across species.

Purpose of the Study:

  • To characterize Ada2 variants in Drosophila and their role in GNAT complexes.
  • To investigate the complex-specific association of Ada-type transcriptional adapter proteins with GNATs.
  • To explore novel functions of Ada2 variants in gene transcription.

Main Methods:

  • Biochemical approaches
  • Cell biological approaches

Related Experiment Videos

  • Polytene chromosome analysis

    • Main Results:

    • Drosophila has two Ada2 variants: dAda2a and dAda2b.
    • dAda2b is a component of Spt-Ada-Gcn5-acetyltransferase (SAGA) complexes.
    • dAda2a associates with dGcn5 independently of SAGA and is found in Gcn5-independent complexes at active transcription sites.
    • This represents the first instance of complex-specific Ada-type protein association with GNATs.
    • Mammalian and fly Ada2 homologues form two distinct functional subgroups.

    Conclusions:

    • The study reveals functional divergence between Drosophila Ada2 variants, dAda2a and dAda2b.
    • dAda2b's role in SAGA complexes and dAda2a's independent associations suggest distinct regulatory mechanisms.
    • The findings highlight novel transcriptional functions for dAda2a and imply conserved functional divergence in mammals.