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Bacillus subtilis DnaG primase stabilises the bacteriophage SPP1 G 40 P helicase‐ssDNA complex
Author(s) -
Ayora Silvia,
Langer Uwe,
Alonso Juan C
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01337-4
Subject(s) - primase , dnag , helicase , bacillus subtilis , dnab helicase , translocase , bacteriophage , chemistry , dna , biology , biophysics , microbiology and biotechnology , biochemistry , dna replication , escherichia coli , genetics , bacteria , circular bacterial chromosome , chromosomal translocation , reverse transcriptase , rna , gene
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 40 P (G 40 P 6 ) in the absence of ATP. G 40 P 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 40 P 6 about 3‐fold, but not the ATPase activity. The results presented here suggest that the DnaG protein stabilises the G 40 P 6 ‐ssDNA complexes.