Interaction in vitro; proteins derived from S2 cell extract.

The C3PO complex was purified from S2 cell extract based on its in vitro RISC enhancing activity and shown to contain the two proteins Trax and trsn. The RISC enhancing activity could be reconstituted by adding purified Trax and trsn to the in vitro RISC assay.

Interaction in vitro; proteins derived from S2 cell extract.

The C3PO complex was purified from S2 cell extract based on its in vitro RISC enhancing activity and shown to contain the two proteins Trax and trsn. The RISC enhancing activity could be reconstituted by adding purified Trax and trsn to the in vitro RISC assay. The Trax and trsn fractions also possessed single-stranded RNase activity.

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

The crystal structure of a truncated CP3O, a complex of truncated versions of trsn and Trax reveals a hexamer composed of two trsn-Trax heterodimers and one trsn homodimer.

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

The estimated molecular mass of the truncated trsn-Trax complex in solution is consistent with the hexamer observed in crystallo. However, the full length trsn-Trax complex, runs at a higher molecular weight in solution than expected if it were also a hexamer.

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

The estimated molecular mass of the truncated trsn-Trax complex in solution is consistent with the hexamer observed in crystallo. However, the full length trsn-Trax complex, runs at a higher molecular weight in solution than expected if it were also a hexamer.

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

Mass-spectrometric measurements of full length trsn-Trax, show that the complex can exist as an octamer with a 6:2 or 5:3 trsn-Trax ratio, with the 6:2 species being the major component. Mass-spectrometric measurements of the truncated trsn-Trax complex, show species with 2:2 , 4:2 and 6:2 trsn-Trax ratios, with the 2:2 and 4:2 species as the major components.

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

Electron microscopy analysis of full length trsn-Trax is consistent with an octamer composed of 4 dimeric molecules of trsn-Trax and trsn-trsn.

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

MORATORIUM:This data was made available \'pre-publication\' and, as such, its use is subject to the specific limitations described in FBrf0235788 for the period of 12 months. Moratorium expires on June 13, 2018.

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

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

MORATORIUM:This data was made available \'pre-publication\' and, as such, its use is subject to the specific limitations described in FBrf0235788 for the period of 12 months. Moratorium expires on June 13, 2018.

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

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

Crystal structure of complex containing Trax E126Q consists of 2 Trax molecules and 2 trsn molecules.

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

In solution the Trax-trsn complex is octomeric with 4:4 stoichiometry.