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

pygo binds only to Lys4-methylated His3. The affinity of pygo PHD domain for the His3 tail when mono-, di- and trimethylated at Lys4 is 21.5 uM, 12.5 uM and 23 uM, respectively.

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

The His3-pygo interaction occurs only when an lgs HD1 peptide, aa 315-348, is present or when F773 of pygo is mutated to W.

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

pygo binds more strongly to the His3 K4me2-modified tail if it also contains the R2me2a modification.

Chemical shifts in pygo residues upon His3 binding, molecular modeling and intermolecular nuclear Overhauser effects (NOEs) indicate that asymmetrically modified Arg2me2a of His3 binds the fly specific \'R2\' groove of the pygo PHD domain.

The pygo PHD domain was expressed as a fusion to the lgs HD1 domain, connected by a flexible linker.

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

pygo binds more strongly to the His3 K4me2-modified tail if it also contains the R2me2a modification.

Rendering fly pygo human-like by the F773W mutation increases its affinity for His3-K4me2 tail from 1 mM to 7.5 uM.

The pygo PHD domain was expressed as a fusion to the lgs HD1 domain, connected by a flexible linker.