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Figure 3 | BMC Biochemistry

Figure 3

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

Figure 3

Binding of SET/TAF-Iβ proteins to histone H3. (A) GST-SET/TAF-Iβ (lane 3), GST-SET/TAF-Iβ constructs (lanes 4, 5, 6, 9, 10) and purified GST (lanes 2, 8) (4 μg each) were immobilised on glutathione-agarose beads and incubated with 4 μg of histone H3. The beads were washed and analysed by SDS-PAGE and Coomassie blue staining. Lanes 1 and 7 indicate the input of histone H3. (B) GST-H3 tail (lanes 1,2) or GST (lanes 3, 4) (2 μg each) were bound on glutathione-agarose beads and incubated with 4 μg of SET/TAFI-β (76–185) (lanes 1, 3) or wild type SET/TAFI-β (lanes 2, 4). The beads were washed and analysed by SDS-PAGE and Coomassie blue staining. The input of SET/TAFI-β and SET/TAFI-β (76–185) is shown in lanes 5, 6. (C)GST (lanes 3, 6), GST-SET/TAF-Iβ (lanes 2, 5), GST-SET/TAF-Iβ (76–185) (lanes 1, 4) (2 μg each) bound on glutathione beads were incubated with 4 μg of purified H3 globular domain (lanes 1, 2, 3) or recombinant histone H3 (lanes 4, 5, 6). Bound proteins were eluted with 20 μl of reduced glutathione and samples were analysed by SDS-PAGE and Coomassie blue staining.

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BMC Biochemistry

ISSN: 1471-2091

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