Source was cell extract of SL2 cell line; bait produced from endogenous gene; prey produced from endogenous gene.

Weak coimmunoprecipitation of MSL proteins compared to the amount of mle immunoprecipitated, suggesting that only a fraction of mle is associated with MSL proteins.

This interaction persists upon RNase treatment.

Source was cell extract of SL2 cell line; bait produced from endogenous gene; prey produced from endogenous gene.

weak interaction

Source was whole cell extracts; bait produced from endogenous gene; prey produced from endogenous gene.

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

Crude nuclear extracts were cross-linked using formaldehyde, sonicated, and subjected to ProteinA affinity purification with rabbit IgG agarose beads eluted under denaturing conditions, and subsequently using streptavidin agarose beads for Bio affinity purification. Purified peptides were eluted by on-bead trypsin digestion and mass spectrometric analysis.

Enrichment of prey protein was compared to input, mock and unrelated BioTAP affinity purifications using a statistical method (Bamse) developed by the authors to control for multiple sources of bias.

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

The interaction of mle with msl-3 is RNA-dependent (strongly reduced by RNase treatment).

The interaction of mle with tagged msl-3 is more efficient when other components of the MSL complex are co-transfected (overexpressed).

Factors were detected on polytene chromosomes using antibodies (to proteins) or biotinylated antisense probes (to ncRNA). The PLA signal develops only if probes to the two factors are in close proximity to each other (within tens of nanometers).

Source was larval salivary gland of wild-type fly line; proteins produced from endogenous gene.