Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey derived from wild-type embryonic extract.

The PN2-3 domain is dispensable for binding to γ-Tubulin.

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

γTub23C coimmunoprecipitates and co-fractionates with Sas-4 as part of the S-γ-TuSC (γ-tubulin small) complex, or the larger S-γ-TuRC (γ-tubulin ring) complex.

Sas-4 complexes were immunoprecipitated from "high-speed lysates" depleted of mature centrosomes and different Sas-4-containing complexes were fractionated on a sucrose gradient.

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

Sas-4 interacts with γTub37C as part of the S-γ-TuSC (γ-tubulin small) complex, or the larger S-γ-TuRC (γ-tubulin ring) complex.

The interaction of Sas-4 with γTub37C is disrupted by the addition of a non-hydrolyzable GTP analog, GMPCPP, to the extract.

The interaction of Sas-4 with γTub37C is increased by the addition of griseofulvin to the extract, a compound that induces hydrolysis of tubulin-bound GTP to GDP.

Coimmunoprecipitation from "high-speed lysates" depleted of mature centrosomes.

Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey derived from wild-type embryonic extract.

Free tubulin can disrupt the interaction of Sas-4 with γTub37C; mutation of the Sas-4 tubulin binding domain prevents this competition.

This interaction is not affected by mutations to the β9-10 surface of the TCP domain: E792A, V800A/I802A or L841K.

Source was cell extract of C131 cell line; bait produced from transfected construct; prey produced from endogenous gene.

Constructs were expressed in acentrosomal cell line derived from Sas-4 null homozygous mutant flies.

Source was embryos of transgenic fly line; bait produced from tagged transgenic construct; prey produced from endogenous gene.

Two gamma-tubulin genes potentially detected by Ab, both curated.