Premium
Protein/DNA architecture of the DNase I hypersensitive region of the Drosophila hsp26 promoter.
Author(s) -
Thomas G. H.,
Elgin S. C.
Publication year - 1988
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1988.tb03058.x
Subject(s) - biology , nucleosome , promoter , heat shock protein , dna , deoxyribonuclease i , gene , microbiology and biotechnology , genetics , histone , gene expression , base sequence
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.