Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey produced as a recombinant fusion protein in bacterial system.

GST-Pym was incubated with bacterial lysate co-expressing mago and tsu.

Interaction in vitro; proteins produced as a recombinant fusion proteins in bacterial system.

Pym (residues 1-58) binds at a surface formed by both mago and the tsu RBD domain (residues 67-154) to form a ternary complex.

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

The N-terminal region of Pym (aa 1-60) is sufficient for binding to tsu only in the presence of cross-linking agent, suggesting a complex with a short half-life. However, the N-terminal and medial regions of Pym (aa 1-152) are sufficient for binding to tsu even in the absence of cross-linking agent, suggesting that the medial region (aa 61-152) stabilizes the complex.

The presence of the Pym C-terminal region (aa 153-208) decreases the Pym-tsu interaction.

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

Pym coimmunoprecipitates mago and tsu, but not btz or ribosomal proteins like eIF4AIII or cap binding proteins like Cbp20.

The Pym-tsu interaction is resistant to RNase treatment, and is thus not mediated indirectly by RNA.

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

Pym coimmunoprecipitates mago and tsu, but not eIF4AIII.