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• W2002411474 abstract "Purified Bacillus subtilis DnaG primase (predicted molecular mass 68.8 kDa) behaves as a monomer in solution. We demonstrate that DnaG physically interacts with bacteriophage SPP1 hexameric helicase G40P (G40P6) in the absence of ATP. G40P6-ATP forms an unstable complex with ssDNA, and by itself carries out ATP-driven translocation along a ssDNA template with low processivity. The presence of DnaG in the reaction mixture increased the helicase activity of G40P6 about 3-fold, but not the ATPase activity. The results presented here suggest that the DnaG protein stabilises the G40P6-ssDNA complexes." @default.
• W2002411474 created "2016-06-24" @default.
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• W2002411474 date "1998-11-13" @default.
• W2002411474 modified "2023-09-27" @default.
• W2002411474 title "Bacillus subtilisDnaG primase stabilises the bacteriophage SPP1 G40P helicase-ssDNA complex" @default.
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• W2002411474 doi "https://doi.org/10.1016/s0014-5793(98)01337-4" @default.
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