The mechanism of forming and stabilizing the open, transcriptionally competent E. coli RNA polymerase-promoter complex was studied through stopped-flow kinetics with fluorescence detection and fast-mixing with radioactivity detection. The intermediates generated from opening the enzyme using T7A1 promoters allowed for kinetic studies. Those results were compared to ones previously calculated using the λPR promoter. The fluorescence experiments confirmed two kinetic phases, a fast followed by a slow. When compared to the T7A1 promoter, λPR forms the open complex slower but it remains open for a longer time. The information gained from studying E. coli RNAP is of relevance for design of new antibiotics and for understanding how human RNAP works due to the enzyme’s highly conserved nature.

Binding kinetics and transition of structural components of RNA polymerase

249th National Meeting (2015)

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