Interaction of bacteriophage T7 gene 4 primase with its template recognition site.

@article{Frick1999InteractionOB,
  title={Interaction of bacteriophage T7 gene 4 primase with its template recognition site.},
  author={David N. Frick and Charles C. Richardson},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 50},
  pages={35889-98}
}
The primase fragment of the bacteriophage T7 63-kDa gene 4 helicase/primase protein contains the 271 N-terminal amino acid residues and lacks helicase activity. The primase fragment catalyzes the synthesis of oligoribonucleotides at rates similar to those catalyzed by the full-length protein in the presence of a 5-nucleotide DNA template containing a primase recognition site (5'-GGGTC-3', 5'-TGGTC-3', 5'-GTGTC-3', or 5'-TTGTC-3'). Although it is not copied into the oligoribonucleotides, the… CONTINUE READING
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Template Binding by T7 DNA Primase

  • R. L. Lechner, C. C. Richardson
  • J. Biol. Chem. 258,
  • 1983

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