A recombinant histone (NLS-H1) containing both the SV40 large T antige
n nuclear localization signal and the carboxy-terminal domain of human
histone H1 degrees was produced in bacteria, NLS-H1-plasmid DNA compl
exes, in the presence of chloroquine, mediated reporter gene transfer
into cultured cells with similar efficiencies as plasmid DNA-cationic
lipid (lipofectin) complexes, NIH-3T3 or COS-7 cells transfected with
NLS-H1-plasmid DNA-lipofectin complexes expressed at Least 20 times mo
re luciferase or had at least 2.5 times more beta-galactosidase-positi
ve cells than those transfected with plasmid DNA-lipofectin complexes,
Foreign gene expression was also improved by other DNA-binding protei
ns and cationic lipid formulations, yet the greatest enhancement was o
btained with complexes containing either NLS-H1 or calf thymus histone
H1, Histone H1-plasmid DNA-lipofectin complexes were internalized by
a greater number of cells than plasmid DNA-lipofectin complexes.