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Bacillus subtilisDnaG primase stabilises the bacteriophage SPP1 G40P helicase-ssDNA complex

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
439
Identifiers
DOI: 10.1016/s0014-5793(98)01337-4
Keywords
  • Phage Biology
  • Spp1
  • Dna Replication
  • Replication Initiation Protein
  • Dna Helicase
  • Dna Primase
Disciplines
  • Biology

Abstract

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 G 40P (G 40P 6) in the absence of ATP. G 40P 6-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 G 40P 6 about 3-fold, but not the ATPase activity. The results presented here suggest that the DnaG protein stabilises the G 40P 6-ssDNA complexes.

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