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Protein-primed replication of bacteriophage phi 29 DNA.

AuthorsSalas, Margarita ; Martín, Gil; Bernad, Antonio; Garmendia Mendizábal, Cristina; Lázaro, José M. ; Zaballos, Ángel; Serrano, Manuel; Otero, María José; Gutiérrez, Julio; Parés, Eulalia; Blasco, María A.; Mellado, J. M.; Hermoso, José Miguel; Blanco, Luis
Issue Date1988
CitationBiochimica et Biophysica Acta - Gene Structure and Expression 951: 419-424 (1988)
AbstractThe replication of phi 29 DNA-protein p3 represents a simple model system to study the protein-priming mechanism of initiation of replication. The phi 29 DNA polymerase involved both in the initiation and elongation steps of phi 29 DNA-protein p3 replication, is a very processive enzyme and it is able to produce strand-displacement in the absence of other proteins. To correlate functional and structural domains in the phi 29 DNA polymerase point mutants in the most carboxyl region of amino-acid homology with other DNA polymerases have been constructed. Most of the mutations had a decreased initiation and elongation activity, but normal 3'----5' exonuclease activity, suggesting that this region contributes to the active domain for initiation and elongation. Point and deletion mutants in the terminal protein have allowed the mapping of one DNA-binding region and two DNA-polymerase-binding regions. The viral protein p6, which stimulates the initiation of replication, binds to a set of specific signals present at both phi 29 DNA ends. A good correlation of binding and stimulation of replication has been obtained by using fragments containing phi 29 DNA-terminal sequences and deletion mutants of protein p6. The viral protein p5 has been shown to bind to single-stranded DNA, to protect the latter against nuclease digetion, and to stimulate phi 29 DNA-protein p3 replication in vitro.
Publisher version (URL)http://dx.doi.org/10.1016/0167-4781(88)90115-7
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