Using paramagnetic and fluorescing labels, we have shown that E. colt
RNA polymerase (E sigma 70) bound with T2 phage DNA undergoes several
specific conformational transitions, which optimize the active site st
ructure at different stages of RNA synthesis. DNA is a conformational
cofactor of RNA polymerase and induces in it specific changes associat
ed with formation of transcriptionally competent complexes. Use of a b
ifunctional fluorescence label, fluorescein dimercuriacetate, allowed
detection of protein regions with relatively independent conformationa
l mobility. The functional significance of the conformational mobility
of local regions in RNA polymerase is discussed.