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dc.contributor.authorOtero, María José-
dc.contributor.authorLázaro, José M.-
dc.contributor.authorSalas, Margarita-
dc.identifier.citationGene 95(1): 25-30 (1990)es_ES
dc.description.abstractDeletions corresponding to the first 5 or 13 amino acids (aa), not counting the initial Met, have been introduced into the N terminus of the phage φ29 protein p6. The activity of such proteins in the in vitro φ29 DNA replication system, their capacity to interact with the φ29 DNA ends, and their interference with the wild type (wt) protein p6 activity have been studied. The initiation activity of protein p6 decreased considerably when 5 aa were deleted and was undetectable when 13 aa were removed. The mutant proteins were unable to specifically interact with the φ29 DNA ends. These results indicate the need of an intact N terminus for the activity of protein p6. However, such N-truncated protein inhibited both the specific binding of the wt protein p6 to the φ29 DNA ends and its activity in φ29 DNA replication.es_ES
dc.description.sponsorshipThis investigation has been aided by Research Grant 5R01 GM27242-10 from the National Institute s of Health, by Grant No.PB87-0323 from Dirección General de Investigación Cientifica y Técnica, and by agrant from Fundación Ramón Areces.es_ES
dc.subjectRecombinant DNAes_ES
dc.subjectPhage γ pL promoteres_ES
dc.subjectProtein p3-dAMP complexes_ES
dc.titleDeletions at the N terminus of bacteriophage ø29 protein p6: DNA binding and activity in ø29 DNA replicationes_ES
dc.description.peerreviewedPeer reviewedes_ES
dc.contributor.funderNational Institutes of Health (US)-
dc.contributor.funderMinisterio de Economía y Competitividad (España)-
dc.contributor.funderFundación Ramón Areces-
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