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Nucleic Acids Research, 1977, Vol. 4, No. 5 1225-1242
© 1977

Articles

Physicochemical studies on interactions between DNA and RNA polymerase. Unwinding of the DNA helix by Escherichia coli RNA polymerase*

James C. Wang, John H. Jacobsen{dagger} and Jean-Marie Saucier{ddagger}

Dep.Chem., Univ. California Berkeley, CA 94720 {dagger}Univ. Chicago Medical School Chicago, IL 60637, USA {ddagger}Institute Gustave-Roussy 94800 Villejuif, France

Received January 1, 1977.

In a medium containing 10 mM Tris, pH 8, 10 mM Mg++,50 mM K+ and 10 mM NH4, the binding of an E. coli RNA polymerase holoenzyme unwinds the DNA helix by about 240° at 37°C. In this medium the total unwinding of the DNA increases linearly with the molar ratio of polymerase to DNA. The number of binding ites at which unwinding can occur is very large. If the K+concentration is increased at 200 mM, the enzyme binds to only a limited number of sites, and the bound and free enzyme molecules do not exchange at an appreciable rate. The unwinding angle of the DNA per bound enzyme in this high salt medium is measured to be 140° at 37°C. The total unwinding angle for a fixed number of bound polymerase molecules per DNA is strongly temperature dependent, and decreases with decreasing temperature.

*Dedicated to Jerome Vinograd. This paper is the second of a series on DNA-RNA polymerase interactions from this laboratory, the first being Hsieh and Wang (1976).


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