Krajewski W A
Laboratory of Biochemistry, Institute of Developmental Biology, Russian Academy of Sciences, Moscow.
Mol Gen Genet. 2000 Feb;263(1):38-47. doi: 10.1007/pl00008674.
We found that Drosophila embryo extract contains a protein activity (or activities) that can destabilize nucleosomes, resulting in increased sensitivity to DNase I, release of nucleosomal supercoiling, high levels of conformational flexibility of DNA and more diffuse micrococcal nuclease digestion patterns. Incorporation of histone H1 did not significantly affect this nucleosome remodelling. Remodelling occurs more efficiently in hyperacetylated chromatin. It was shown previously that hyperacetylated chromatin, reconstituted in a Drosophila embryo cell-free system, exhibits increased DNase I sensitivity and a high degree of conformational flexibility of DNA. The present data suggest that the more diffuse structure of acetylated chromatin is a result of chromatin remodelling by protein activities in the Drosophila embryo extract.
我们发现果蝇胚胎提取物含有一种（或多种）能够使核小体不稳定的蛋白质活性物质，这会导致对DNase I的敏感性增加、核小体超螺旋的释放、DNA的高度构象灵活性以及更弥散的微球菌核酸酶消化模式。组蛋白H1的掺入对这种核小体重塑没有显著影响。在高度乙酰化的染色质中，重塑过程更有效。先前的研究表明，在果蝇胚胎无细胞系统中重构的高度乙酰化染色质表现出对DNase I的敏感性增加以及DNA的高度构象灵活性。目前的数据表明，乙酰化染色质更弥散的结构是果蝇胚胎提取物中蛋白质活性对染色质进行重塑的结果。
