Recombinant histones were separately expressed and purified under denaturing conditions to directly solubilize inclusion bodies, then mixed (1mg each) and purified by size exclusion chromatography.

Recombinant His2A, His2B, His3 and His4 could be purified as a histone octamer complex.

His2A-His2B heterodimers were also observed using this assembly protocol.

Interaction in vitro; proteins produced as a recombinant fusion proteins in bacterial system.

Interaction in vitro; proteins produced as a recombinant fusion proteins in bacterial system.

Estimated size of cross-linked moiety is consistent with a heterodimer.

Strong interaction.

Source was Kc167 cells; proteins produced from transfected constructs.

Cells treated with 400uM oleic acid to induce lipid droplet formation in cells.

Strong interaction.

Source was Kc167 cells; proteins produced from transfected constructs.

Cells treated with 400uM oleic acid to induce lipid droplet formation in cells.