Crossref journal-article
Wiley
FEBS Letters (311)
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.

Bibliography

Ayora, S., Langer, U., & Alonso, J. C. (1998). Bacillus subtilis DnaG primase stabilises the bacteriophage SPP1 G40P helicase‐ssDNA complex. FEBS Letters, 439(1–2), 59–62. Portico.

Authors 3
  1. Silvia Ayora (first)
  2. Uwe Langer (additional)
  3. Juan C Alonso (additional)
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Dates
Type When
Created 23 years, 1 month ago (July 25, 2002, 1:53 p.m.)
Deposited 1 year, 11 months ago (Sept. 17, 2023, 1:36 a.m.)
Indexed 1 year, 2 months ago (June 14, 2024, 12:36 p.m.)
Issued 26 years, 9 months ago (Nov. 13, 1998)
Published 26 years, 9 months ago (Nov. 13, 1998)
Published Online 26 years, 9 months ago (Dec. 3, 1998)
Published Print 26 years, 9 months ago (Nov. 13, 1998)
Funders 0

None

@article{Ayora_1998, title={Bacillus subtilis DnaG primase stabilises the bacteriophage SPP1 G40P helicase‐ssDNA complex}, volume={439}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/s0014-5793(98)01337-4}, DOI={10.1016/s0014-5793(98)01337-4}, number={1–2}, journal={FEBS Letters}, publisher={Wiley}, author={Ayora, Silvia and Langer, Uwe and Alonso, Juan C}, year={1998}, month=nov, pages={59–62} }