Ada2b, but not Ada2a, copurifies with Taf4, Gcn5 and e(y)1 in a large complex, approximately 2 MDa in size.

Source was embryonic nuclear extract of wild-type fly line; bait produced from endogenous gene; prey produced from endogenous gene.

Embryonic nuclear extract was first fractionated on a heparin column, then size fractioned by Superose 6 gel filtration.

e(y)1 coimmunoprecipitates with Ada2b, but not with Ada2a.

Source was nuclear extract of S2 cell line; bait produced from endogenous gene; prey produced from endogenous gene.

Source was nuclear extract of S2 cell line; bait produced from transfected construct; prey produced from endogenous gene.

The Drosophila SAGA complex is composed of the following subunits: Gcn5, Ada2b, dik, Sgf29, CG6506, Ada1-2, Spt3, Spt20, Nipped-A, e(y)1 (Taf9), Taf10b, Taf12, wda, Saf6, not, Sgf11, e(y)2 and Atxn7.

Tandem affinity purification of bait and identification of prey by MudPIT.

Source was embryonic nuclear extract of transgenic fly line; bait produced from tagged transgenic construct in nervous system (elav-GAL4); prey produced from endogenous gene.

All SAGA subunits were present in purifications from both muscle and neuronal cells.

Proteins that non-specifically bind FLAG beads were identified in control purifications from untagged extract (OregonR) and excluded from further analysis.

Source was embryonic nuclear extract of transgenic fly line; bait produced from tagged transgenic construct in muscle (Mef2-GAL4); prey produced from endogenous gene.

All SAGA subunits were present in purifications from both muscle and neuronal cells.

Proteins that non-specifically bind FLAG beads were identified in control purifications from untagged extract (OregonR) and excluded from further analysis.