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Nucleic Acids Research, 1978, Vol. 5, No. 6 1845-1862
© 1978

Articles

Subunit topography of RNA polymerase (E. coli) in the complex with DNA

M. Okada, J. Vergne and J. Brahms

Institut de Recherche en Biologie Moléculaire (CNRS) 2 Place Jussieu, Paris 5eme, France

Received March 1, 1978. E. Coli RNA polymerase binding to different DNAs (from E. Coli, 5-bromodeoxyuridine (BrdUrd) substituted DNA and poly [d(BrU-A)] was induced with ultraviolet (U.V.) light to form protein-DNA crosslinked complexes. Two independent methods of analysis, polyacrylamide gel electrophoresis in SDS and chloroform extraction indicated the formation of a stable complex between the enzyme and DNA. The complexes were formed under different ionic strength conditions, at low enzyme to DNA ratios in order to approach the conditions of specific binding. In contrast there was no crosslinking of the complex in 1 M KCl solution which dissociates the enzyme from DNA. The efficiency of formation of strongly bound complex was found to be much higher with holoenzyme than with core enzyme. The following results were obtained: 1) The large subunits ß and ß' were found to be bound to DNA. 2) Relatively small amount of {sigma} subunit were bound to DNA while {sigma} subunits were essentially not attached to DNA. The high binding affinity of ß and ß' subunits was also observed in the studies of isolated subunits. These results lead to a model of enzyme-DNA complex in which the large ß and ß' subunits provide the contacts between the RNA polymerase and the DNA.


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