The temperature-dependent conformational transitions of E. coil RNA po
lymerase complexes with the bacteriophage T7 D promoter were studied.
The topology of two types of conformers was assessed by DNase I footpr
inting. Enzymatic testing of the promoter structure revealed structura
l changes in the temperature range considered. The data obtained testi
fy that the physicochemical properties of the promoter DNA may be the
basis of the structural-conformational rearrangements in the transcrip
tional complex and, therefore, be important for the differentiated reg
ulation of gene activity.