Temperature dependent release of beta-beta' subunits of DNA dependent RNA polymerase from the folded chromosome of a dnaAts mutant of Escherichia coli.

DNA-dependent RNA polymerase has been found to be preferentially released at 43 degrees C from the folded nucleoids of an E. coli dnaAts mutant when compared with the same nucleoids at 30 degrees C or with nucleoids of a dnaA+ strain at either 30 degrees or 43 degrees C. The polypeptides released are identical in molecular weight with those of the beta and beta' constituent polypeptides of the core enzyme of a known E. coli RNA polymerase. In addition, these polypeptides are precipitated by specific anti-RNA polymerase rabbit IgG. The implications of the interactions of RNA polymerase with the dnaA gene product are discussed.