Involvement of residues of the ϕ29 terminal protein intermediate and priming domains in the formation of a stable and functional heterodimer with the replicative DNA polymerase

@inproceedings{Prado2012InvolvementOR,
  title={Involvement of residues of the ϕ29 terminal protein intermediate and priming domains in the formation of a stable and functional heterodimer with the replicative DNA polymerase},
  author={Alicia del Prado and Laurentino Villar and Miguel de Vega and Margarita Salas},
  booktitle={Nucleic acids research},
  year={2012}
}
Bacteriophage Φ29 genome consists of a linear double-stranded DNA with a terminal protein (TP) covalently linked to each 5' end (TP-DNA) that together with a specific sequence constitutes the replication origins. To initiate replication, the DNA polymerase forms a heterodimer with a free TP that recognizes the origins and initiates replication using as primer the hydroxyl group of TP residue Ser232. The 3D structure of the DNA polymerase/TP heterodimer allowed the identification of TP residues… CONTINUE READING

References

Publications referenced by this paper.
SHOWING 1-10 OF 38 REFERENCES

DNA polymerase residue Ser122, a single-stranded DNA ligand for 30-50 exonucleolysis, is required to interact with the terminal protein

M. de Vega, L. Blanco, M. Salas
  • J. Biol. Chem.,
  • 1998
VIEW 5 EXCERPTS
HIGHLY INFLUENTIAL

Functional characterization of highly processive protein-primed DNA polymerases from phages Nf and GA-1, endowed with a potent strand displacement capacity

E. Longás, M. de Vega, J. M. Lázaro, M. Salas
  • Nucleic Acids Res.,
  • 2006
VIEW 2 EXCERPTS

DNA polymerase-terminal protein interaction. Involvement of residues specifically conserved among protein-primed DNA polymerases

I. Rodrı́guez, J. M. Lázaro, M. Salas, M. de Vega
  • J. Mol. Biol.,
  • 2004
VIEW 1 EXCERPT

f 29 DNA polymeraseterminal protein interaction . Involvement of residues specifically conserved among proteinprimed DNA polymerases

I. Rodrı́guez, J. M. Lázaro, M. Salas, M. de Vega
  • J . Mol . Biol .
  • 2004

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