Thomas G H, Elgin S C
Department of Biology, Washington University, St. Louis, MO 63130.
EMBO J. 1988 Jul;7(7):2191-201. doi: 10.1002/j.1460-2075.1988.tb03058.x.
Genomic footprinting on the Drosophila hsp26 promoter in isolated nuclei has shown that a TATA box binding factor is present before and after induction by heat shock, while three of the seven heat shock consensus sequences 5' of the gene are occupied (presumably by heat shock factor, HSF) specifically on heat shock. The sites of HSF interaction are separated by greater than 200 bp of which approximately 150 bp are bound to the surface of a nucleosome. The juxtaposition of these various macromolecules on the DNA suggests a basis for the major DNase I hypersensitive site 5' of hsp26 and a novel tertiary structure for the promoter complex.
对分离细胞核中果蝇热休克蛋白26(hsp26)启动子进行的基因组足迹分析表明,在热休克诱导前后均存在一种TATA盒结合因子,而该基因5'端七个热休克共有序列中的三个在热休克时被特异性占据(推测被热休克因子HSF占据)。HSF相互作用的位点被超过200 bp的间隔分开,其中约150 bp与核小体表面结合。这些不同大分子在DNA上的并列排列为hsp26基因5'端主要的DNA酶I超敏位点提供了基础,并为启动子复合物提供了一种新的三级结构。