Pruss D, Wolffe A P
Laboratory of Molecular Embryology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892.
Biochemistry. 1993 Jul 13;32(27):6810-4. doi: 10.1021/bi00078a002.
We describe histone-DNA cross-linking in a nucleosome core containing a Xenopus borealis somatic 5S rRNA gene. Histones H3 and H4 are cross-linked to DNA within 30 bp to either side of the dyad axis. Histones H2A/H2B and H3 are cross-linked to DNA where it enters and exists, wrapping around the histone octamer. These latter interactions extend for 80 bp to one side of the dyad axis of the nucleosome core, including the entire binding site for transcription factor TFIIIA. These extensive interactions with linker DNA might account for inhibition of TFIIIA binding and also might assist in the folding of internucleosomal DNA within the chromatin fiber.
我们描述了在含有北极爪蟾体细胞5S rRNA基因的核小体核心中的组蛋白-DNA交联。组蛋白H3和H4在二分体轴两侧30 bp范围内与DNA交联。组蛋白H2A/H2B和H3在DNA进入和离开核小体、围绕组蛋白八聚体的位置与DNA交联。这些后期的相互作用在核小体核心二分体轴的一侧延伸80 bp，包括转录因子TFIIIA的整个结合位点。与连接DNA的这些广泛相互作用可能是TFIIIA结合受到抑制的原因，也可能有助于染色质纤维内核小体间DNA的折叠。
