Identification of distinct SET/TAF-Iβ domains required for core histone binding and quantitative characterisation of the interaction

Table 1 Relative affinities of SET-TAFI-β and its deletion mutants for H3

Binding of the various SET/TAF-Iβ deletion mutants with histone H3 was followed by monitoring the intensity of the fluorescence emitted by the tryptophan residues of SET/TAF-Iβ polypeptides upon addition of increasing amounts of calf thymus histone H3. The dissociation constant (K_d) for the complexes formed was estimated by non-linear regression analysis (KaleidaGraph, Synergy Software), as indicated in Methods.

ISSN: 1471-2091