Gcn5 interacts with both Ada2a and Ada2b.

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

Gcn5 interacts with both Ada2a and Ada2b.

Source was yeast cell line; bait produced as transgenic fusion protein; prey produced as transgenic fusion protein (prey was previously cloned reagent).

Two-hybrid system: yeast LexA-BD/GAL4-AD

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

Ada2a and Gcn5 copurify in a complex of about 440 kDa, much smaller than the approximately 2 MDa SAGA complex.

Nuclear extract was first fractionated by anion exchange, then by size exclusion chromatography.

Ada2a and Gcn5 copurify in a complex of about 440 kDa, much smaller than the approximately 2 MDa SAGA complex.

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

Immunoprecipitation of proteins in size fractionated extract containing complexes of about 440 kDa.

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

Tandem affinity purification of bait protein (Protein A, then CBP purification) and MudPIT identification of prey proteins.

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

Tandem affinity purification of bait protein (Protein A, then CBP purification) and MudPIT identification of prey proteins.

Source was yeast cell line; bait produced as transgenic fusion protein; prey produced as transgenic fusion protein (prey was previously cloned reagent).

Two-hybrid system: yeast lexA-BD/GAL4-AD

Bait expressed in stably transfected cell lines.

Prey endogenous to nuclear extract.

Proteins derived from affinity-purified TAP-tagged Ada2a complexes in nuclear extract.

Pcaf coimmunoprecipitates and cofractionates with Ada2a in size exclusion chromatography as part of 1.3-1.8 MDa ATAC histone acetyltransferase complex.

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

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

Tagged complexes were isolated by affinity purification and separated by size exclusion chromatography before mass spectrometry.

Interact as part of the ATAC histone acetyltransferase complex.

Bait expressed in stably transfected cells.

Prey endogenous to nuclear extract.