The issue of whether histone H1 possesses specificity of binding to ce
rtain nucleotide sequences in DNA is of fundamental importance to the
suggested role of the linker histone in the regulation of gene transcr
iption. The purpose of the present study was to reinvestigate the spec
ificity of binding of histone H1 to the putative nuclear factor I (NFI
) recognition sequence suggested by a previous report in the literatur
e. The interaction of purified mouse liver histone HI with a synthetic
oligonucleotide representing the natural NFI binding site from the ad
enovirus 2 origin of replication cloned in pBR322 has been studied by
filter binding and a solid-phase procedure performed on nitrocellulose
filter-immobilized protein dots. No indication of specific interactio
ns of the lysine-rich histone H1 with the NFI recognition sequence was
obtained.