Abstract
Purified RNA polymerase, DNA polymerase III and unwinding protein of Escherichia coli catalyze limited rifampicin sensitive fd or ØX 174 DNA-dependent DNA synthesis. A protein has been partially purified from E. coli which stimulates rifampicin sensitive dXMP incorporation in this system 20 to 30 fold. This protein also stimulates DNA synthesis catalyzed by DNA polymerases I and II; the stimulation occurs in reactions primed with natural and synthetic DNAs as well as RNA-DNA hybrids. The protein is not a product of the known dna genes. In contrast to the above system of purified enzymes, rifampicin sensitive dXMP incorporation in crude extracts of E. coli is specifically dependent on fd but not ØX 174 DNA. An additional factor has been isolated from extracts of E. coli which restores specificity to the purified rifampicin sensitive system by preventing ØX 174 DNA from serving as a template.
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