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pubmed-article:9849877pubmed:abstractTextPurified 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.lld:pubmed
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pubmed-article:9849877pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:9849877pubmed:year1998lld:pubmed
pubmed-article:9849877pubmed:articleTitleBacillus subtilis DnaG primase stabilises the bacteriophage SPP1 G40P helicase-ssDNA complex.lld:pubmed
pubmed-article:9849877pubmed:affiliationDepartamento de Biotecnología Microbiana, Centro Nacional de Biotecnología, CSIC, Campus Universidad Autónoma de Madrid, Cantoblanco, Madrid, Spain.lld:pubmed
pubmed-article:9849877pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9849877pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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