Interaction in vitro; bait peptide source unspecified; prey derived from Nurf complex reconstituted from proteins expressed in a baculovirus and Sf9 cell system.

Caf1-55 preferentially binds unmodified His3.

His3, His4, Caf1-55 complex reconstituted in vitro and subjected to analytical ultracentrifugation, interaction captured pairwise.

Interaction in vitro; peptide synthesized in vitro; recombinant protein produced in baculovirus and insect cell system.

Interaction in vitro; bait produced as recombinant protein in baculovirus and insect cell system; prey peptide synthesized in vitro.

Trimethylation at His3 K4 disrupts interaction Kd>500μM, trimethylation at His3 K9 decreases interaction Kd=22μM.

Interaction in vitro; bait peptides synthesized in vitro; prey produced as recombinant protein in baculovirus and insect cell system.

His3, His4 heterodimer used as bait, interaction captured pairwise.

His3, His4, Caf1-55 complex reconstituted in vitro and subjected to gel filtration, interaction captured pairwise.

Interaction in vitro; peptide synthesized in vitro; recombinant protein produced in baculovirus and insect cell system.

Interaction in vitro; bait produced as a recombinant fusion protein in a baculovirus and insect cell system; prey peptide chemically synthesized and labeled in vitro.

His3 binds Caf1-55 and a Caf1-55-Su(z)12 complex similarly suggesting the two interactions are not interdependent. Methylation at K4 of His3 decreases its interaction with a Caf1-55-Su(z)12 complex.

Interaction in vitro; bait produced as a recombinant fusion protein in a baculovirus and insect cell system; prey peptide chemically synthesized.

The interaction between His3 and Caf1-55 was probed in the context of a Caf1-55-Su(z)12 complex. Methylation at K4 of His3 decreases its interaction with a Caf1-55-Su(z)12 complex.

The antibody used was raised against purified core histones.

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