Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/38686
Título : Mechanism of stimulation of DNA replication by bacteriophage ø29 SSB protein p5
Autor : Blasco, María A., Bernad, Antonio, Blanco, Luis, Salas, Margarita
Fecha de publicación : 25-Apr-1991
Editor: American Society for Biochemistry and Molecular Biology
Citación : Journal of Biological Chemistry 266: 7904-7909 (1991)
Resumen: The phi 29 DNA polymerase, an alpha-like DNA polymerase, shows an inorganic pyrophosphate-dependent degradative activity with similar requirements to the corresponding one of Escherichia coli DNA polymerase I: (a) it requires a high concentration of inorganic pyrophosphate and is reversed by polymerization; (b) like DNA polymerization, it needs a duplex DNA with protruding 5' single-strand; (c) it acts in the 3' to 5' direction releasing free dNTPs, thus, it can be considered as the reversal of polymerization; (d) although a correctly base-paired 3' primer terminus is the preferred substrate, the pyrophosphorolytic activity is able to remove mismatched 3' ends. In agreement with the structural and functional model previously proposed for the phi 29 DNA polymerase, the analysis of point mutations has revealed that the pyrophosphorolytic activity, like the polymerization activity, is located at the C-terminal portion of the molecule, involving the amino acid motif YCDTD, highly conserved in alpha-like DNA polymerases. Furthermore, the analysis of phi 29 DNA polymerase mutants indicates that pyrophosphorolysis, like DNA polymerization, also requires an efficient translocation of the enzyme along the template.
Versión del editor: http://www.jbc.org/content/266/12/7904.full.pdf+html
URI : http://hdl.handle.net/10261/38686
ISSN: 0021-9258
1083-351X
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