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

In testis, jar coimmunoprecipitates Acam, but not Cam. This interaction is probably Calcium-dependent, as the interaction is inhibited in the presence of EGTA.

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 GAL4-BD/GAL4-AD

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

Acam binds to jar peptides more strongly in the presence of Calcium.

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

The C-lobe of Acam binds to both the \'Insert 2\' and \'IQ\' motif peptides of the jar protein.

The N-lobe of Acam does not change conformation in the presence of either the \'Insert 2\' or \'IQ\' motifs. However, the Acam N-lobe\'s structure resembles the structure of the Cam N-lobe bound to the \'IQ\' motif. Given functional studies of the Acam N-lobe in other studies, the authors infer that the Acam N-lobe binds to the jar \'IQ\' motif without changing its conformation.

Mass spectrometry was used to examine dynamic changes in Acam upon interaction with the binding motifs of jar.

Interaction in vitro; Acam produced as a recombinant fusion protein in bacterial system; jar peptide chemically synthesized.