Yaneva J N, Zlatanova J S
Institute of Molecular Biology, Bulgarian Academy of Sciences, Sofia.
Biochimie. 1993;75(6):497-500. doi: 10.1016/0300-9084(93)90116-a.
The issue of whether histone H1 possesses specificity of binding to certain nucleotide sequences in DNA is of fundamental importance to the suggested role of the linker histone in the regulation of gene transcription. The purpose of the present study was to reinvestigate the specificity of binding of histone H1 to the putative nuclear factor I (NFI) recognition sequence suggested by a previous report in the literature. The interaction of purified mouse liver histone H1 with a synthetic oligonucleotide representing the natural NFI binding site from the adenovirus 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 interactions of the lysine-rich histone H1 with the NFI recognition sequence was obtained.
组蛋白H1是否具有与DNA中特定核苷酸序列结合的特异性这一问题,对于连接组蛋白在基因转录调控中所起的假定作用至关重要。本研究的目的是重新研究组蛋白H1与先前文献报道中提出的假定核因子I(NFI)识别序列的结合特异性。通过滤膜结合以及在硝酸纤维素滤膜固定的蛋白质点上进行的固相程序,研究了纯化的小鼠肝脏组蛋白H1与代表克隆于pBR322的腺病毒2复制起点天然NFI结合位点的合成寡核苷酸之间的相互作用。未获得富含赖氨酸的组蛋白H1与NFI识别序列发生特异性相互作用的迹象。