Interaction in vitro; bait peptide synthesized in vitro; prey derived from wild-type embryonic extract.

Sfmbt binds to His4 histone tail that is monomethylated at Lys 20 (Kd = 8 uM) or dimethylated at Lys 20 (Kd = 12 uM). His4 peptides that are unmodified or trimethylated at Lys 20 bind with over ten-fold reduced affinity. No binding was observed for His4 peptides acetylated at residue Lys 16.

Interaction in vitro; His4 peptide synthesized in vitro; Sfmbt produced as a recombinant fusion protein in bacterial system.

A methylated lysine of a single His4 peptide binds the aromatic pocket in the fourth MBT domain of Sfmbt. Additional contacts are made between Sfmbt and flanking His4 residues.

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

Sfmbt binds to various mono- and dimethylated lysines in His3 and His4 with very low micromolar affinity, but not to unmethylated or trimethylated peptides.

The lack of Sfmbt specificity for different His3 and His4 mono- or dimethylated lysine residues observed in this study contrasts with work in Klymenko et al., 2006 (FBrf0190547) and may reflect technical differences.

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

Sfmbt binds to various mono- and dimethylated lysines in His3 and His4 with very low micromolar affinity, but not to unmethylated or trimethylated peptides.

The lack of Sfmbt specificity for different His3 and His4 mono- or dimethylated lysine residues observed in this study contrasts with work in Klymenko et al., 2006 (FBrf0190547) and may reflect technical differences.

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

Sfmbt and His4 bind with micromolar affinity, Kd = 16.7 uM.