Summary
The DNA polymerase of Ustilago maydis is stimulated by a DNA binding protein from the same organism. Analysis of this stimulation shows that there is an increase in affinity for both substrates of the reaction. The apparent Km for deoxynucleoside triphosphates is decreased 3 fold, and that for denatured DNA by 4 fold. In both cases the maximum velocity (Vmax) is increased 1.2 to 1.4 fold. It is suggested that the variability in the affinity of the enzyme for deoxynucleoside triphosphates mediated by the binding protein may provide the basis for the UV sensitivity of pyrimidine auxotrophs in this organism.
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Communicated by B.A. Bridges
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Yarranton, G.T., Moore, P.D. & Spanos, A. The influence of DNA binding protein on the substrate affinities of DNA polymerase from Ustilago maydis: One polymerase implicated in both DNA replication and repair. Molec. Gen. Genet. 145, 215–218 (1976). https://doi.org/10.1007/BF00269596
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DOI: https://doi.org/10.1007/BF00269596