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Título: | Characterization and purification of a phage ø29 coded DNA polymerase required for the initiation of replication |
Autor: | Blanco, Luis CSIC ORCID ; Salas, Margarita CSIC ORCID | Fecha de publicación: | 1-sep-1984 | Editor: | National Academy of Sciences (U.S.) | Citación: | Proceedings of the National Academy of Sciences 81(17): 5325-5329 (1984) | Resumen: | The phage phi 29 protein p2, required for the formation of the protein p3-dAMP initiation complex, has been purified from Escherichia coli cells harboring a gene 2-containing recombinant plasmid. The purified protein p2, of molecular weight 68,000, had a specific DNA polymerase activity that elongated the p3-dAMP initiation complex when phi 29 DNA-protein p3 was used as template. In addition, the purified protein p2 was active in catalyzing the initiation reaction when complemented with phi 29 mutant sus2-infected Bacillus subtilis or plasmid-containing E. coli extracts providing protein p3, in the presence of phi 29 DNA-protein p3 as template. However, when purified protein p3 was used in the complementation assay, a very low amount of initiation complex was formed; addition of extracts from uninfected B. subtilis or E. coli strongly stimulated the initiation reaction, indicating that, in addition to proteins p2 and p3 and the phi 29 DNA-protein p3 template, some host factor(s) is required for the formation of the p3-dAMP initiation complex. The results show that phage phi 29 encodes a DNA polymerase that is required at the initiation step of protein-primed DNA synthesis. | Versión del editor: | http://www.pnas.org/content/81/17/5325.abstract | URI: | http://hdl.handle.net/10261/38574 | ISSN: | 0027-8424 |
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