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dc.contributor.authorZaballos, Ángel-
dc.contributor.authorSalas, Margarita-
dc.date.accessioned2011-08-01T08:56:21Z-
dc.date.available2011-08-01T08:56:21Z-
dc.date.issued1989-12-25-
dc.identifier.citationNucleic Acids Research 17(24): 10353-10366 (1989)es_ES
dc.identifier.issn0305-1048-
dc.identifier.urihttp://hdl.handle.net/10261/38161-
dc.description.abstractDeletion mutants at the amino- and carboxyl-ends of the ø29 terminal protein, as well as internal deletion and substitution mutants, whose ability to prime the initiation of ø29 DNA replication was affected to different extent, have been assayed for their capacity to interact with DNA or with the ø29 DNA polymerase. One DNA binding domain at the amino end of the terminal protein has been mapped. Two regions involved in the binding to the DNA polymerase, an internal region near the amino-terminus and a carboxyl-terminal one, have been also identified. Interaction with both DNA and ø29 DNA polymerase are required to led to the formation of terminal protein-dAMP initiation complex to start ø29 DNA replication.es_ES
dc.language.isoenges_ES
dc.publisherOxford University Presses_ES
dc.rightsopenAccesses_ES
dc.titleFunctional domains in the bacteriophage ø29 terminal protein for interaction with the ø29 DNA polymerase and with DNAes_ES
dc.typeartículoes_ES
dc.identifier.doi10.1093/nar/17.24.10353-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1093/nar/17.24.10353es_ES
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