pho coimmunoprecipitated Ino80, Sfmbt, rept and pont, but not the polycomb group proteins (E(z), Pc, Su(z)12, Scm) or the nucleosome remodeling factor dom.

Gradient sedimentation of nuclear extracts indicates that Sfmbt and Ino80 exist in distinct pho-containing complexes.

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

Sfbmt coimmunoprecipitates pho and phol, but not Ino80 or other polycomb group proteins (Ph, Pc, Scm or Su(z)12). Sfbmt and pho are part of the Pho-repressive complex (PhoRC).

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

Source was cell extract of baculovirus-infected Sf9 cell line; bait produced from transfected construct; prey produced from transfected construct.

In this assay, pho and Sfmbt form a stable complex with each other, but not with other proteins identified by mass spectrometry with TAP-tagged pho : rept or pont.

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

pho interacts with Sfmbt, but not other MBT domain-containing proteins l(3)mbt or Scm.

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

A D917E mutation in Sfmbt does not affect binding to pho.

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

pho and Sfmbt bind with nanomolar affinity, Kd = 18 nM.

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

pho and Sfmbt bind with nanomolar affinity, Kd = 18 nM.

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

Sfmbt coimmunoprecipitates pho but not another polycomb group protein, E(z).

Sfmbt coimmunoprecipitates pho, Rpd3, HP1b, Nap1 and ocm in three independent purifications: the PhoRC-L complex.

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

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

The Sfmbt-pho interaction decreases upon heat shock.

The PhoRC complex consists of Sfmbt and pho.

Interaction in vitro; bait and prey produced recombinant fusion proteins in baculovirus and insect cell system.