The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo.

摘要: We have used a combination of kinetic measurements and targeted mutations to show that the C-terminal domain is required for high-affinity binding histone H1 chromatin, phosphorylations can disrupt by affecting secondary structure C terminus. By measuring fluorescence recovery after photo-bleaching profiles green fluorescent protein-histone proteins in living cells, we find deletion N terminus only modestly reduces affinity. Deletion terminus, however, almost completely eliminates H1.1 binding. Specific identified Thr-152 Ser-183 as novel regulatory switches control vivo. It remarkable single amino acid substitution with glutamic was effective truncation 151 destabilizing found modifications affect dramatically but little or no influence on charge distribution overall net this domain. A comparison individual point mutants, when reviewed collectively, cannot be reconciled simple charge-dependent mechanisms function linker histones.