Bacillus subtilis DnaG primase stabilises the bacteriophage SPP1 G40P helicase-ssDNA complex.
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.
Ayora
S
S
Departamento de Biotecnología Microbiana, Centro Nacional de Biotecnología, CSIC, Campus Universidad Autónoma de Madrid, Cantoblanco, Madrid, Spain.
Langer
U
U
Alonso
J C
JC
D000251:Adenosine Triphosphatases / Q000378:metabolism; D001412:Bacillus subtilis / Q000201:enzymology* / Q000378:metabolism; D001435:Bacteriophages / Q000201:enzymology / Q000378:metabolism; D004265:DNA Helicases / Q000378:metabolism*; D019915:DNA Primase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D004277:DNA, Single-Stranded / Q000378:metabolism*; D014764:Viral Proteins
D004277:DNA, Single-Stranded; D014764:Viral Proteins; D019915:DNA Primase; D000251:Adenosine Triphosphatases; D004265:DNA Helicases; C115901:G40P helicase protein, Bacteriophage SPP1