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Nucleic Acids Research, 1983, Vol. 11, No. 18 6369-6380
© 1983

ENZYMOLOGY

Mechanism of stimulation by a specific protein factor of de novo DNA synthesis by mouse DNA replicase with fd phage single stranded circular DNA

Tatsuo Yagura, Tomoko Kozu and Takeshi Seno

Department of Immunology and Virology, Saitama Cancer Center Research Institute 818 Komuro, Ina-machi, Kitaadachi-gim, Saitama 362, Japan

Received June 20, 1983. Revised August 15, 1983. Accepted August 15, 1983.

Mouse DNA replicase is a functional multienzyme complex consisting of DNA polymerase and DNA primase.The DNA and initiator RNA syntheses by DNA replicase with single stranded DNA as template are stimulated by a stimulating factor (T.Yagura.T.Kozu and T.Seno,1982,J.Biochem.(Tokyo).91,607–618).The action mechanism of the stimulating factor on this novel DNA synthesis with fd phage single stranded circular DNA as template was studied.The stimulating factor directly stimulated initiator RNA synthesis but did not change the length of either initiator RNA (8 to 10 nucleotides long) or the product DNA (300 to 1,000 nucleotidee long).Kinetic studies and analysis of the products by neutral agarose gel electrophoresis show that the stimulating factor increased the affinity of DNA replicase for template DNA without changing the apparent Km values for deoxy-and ribonucleotide substrates.Thus, in combination with a sufficient amount of the stimulating factor, DNA replicase quantitatively converted the template DNA to the position of double-stranded circular replicative form II DNA, as shown by agarose gel electrophoresis.


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