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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Pérez-Arnáiz, Patricia | - |
dc.contributor.author | Longás, Elisa | - |
dc.contributor.author | Villar, Laurentino | - |
dc.contributor.author | Lázaro, José M. | - |
dc.contributor.author | Salas, Margarita | - |
dc.contributor.author | Vega, Miguel de | - |
dc.date.accessioned | 2008-10-20T15:05:15Z | - |
dc.date.available | 2008-10-20T15:05:15Z | - |
dc.date.issued | 2007-10-02 | - |
dc.identifier.citation | Nucleic Acids Research 2007 35(21):7061-7073 | en_US |
dc.identifier.issn | 0305-1048 | - |
dc.identifier.uri | http://hdl.handle.net/10261/7901 | - |
dc.description.abstract | To initiate phi 29 DNA replication, the DNA polymerase has to form a complex with the homologous primer terminal protein (TP) that further recognizes the replication origins of the homologous TP-DNA placed at both ends of the linear genome. By means of chimerical proteins, constructed by swapping the priming domain of the related phi 29 and GA-1 TPs, we show that DNA polymerase can form catalytically active heterodimers exclusively with that chimerical TP containing the N-terminal part of the homologous TP, suggesting that the interaction between the polymerase TPR-1 subdomain and the TP N-terminal part is the one mainly responsible for the specificity between both proteins. We also show that the TP N-terminal part assists the proper binding of the priming domain at the polymerase active site. Additionally, a chimerical phi 29 DNA polymerase containing the GA-1 TPR-1 subdomain could use GA-1 TP, but only in the presence of phi 29 TP-DNA as template, indicating that parental TP recognition is mainly accomplished by the DNA polymerase. The sequential events occurring during initiation of bacteriophage protein-primed DNA replication are proposed | en_US |
dc.description.sponsorship | P.P-A. and E.L. were predoctoral fellows of the Spanish Ministry of Education and Science. Spanish Ministry of Education and Science (BFU 2005-00733 to M.S.); Institutional grant from Fundación Ramón Areces to the Centro de Biología Molecular ‘Severo Ochoa’. Funding to pay the Open Access publication charges for this article are provided by research grant BFU 2005-00733 from the Spanish Ministry of Education and Science | en_US |
dc.format.extent | 800907 bytes | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | en_US |
dc.publisher | Oxford University Press | en_US |
dc.rights | openAccess | en_US |
dc.subject | Phi 29 DNA polymerase | en_US |
dc.subject | Phi 29 TP-DNA | en_US |
dc.title | Involvement of phage phi 29 DNA polymerase and terminal protein subdomains in conferring specificity during initiation of protein-primed DNA replication | en_US |
dc.type | artículo | en_US |
dc.identifier.doi | 10.1093/nar/gkm749 | - |
dc.description.peerreviewed | Peer reviewed | en_US |
dc.relation.publisherversion | http://dx.doi.org/10.1093/nar/gkm749 | en_US |
dc.identifier.e-issn | 1362-4962 | - |
dc.contributor.funder | Ministerio de Educación y Ciencia (España) | - |
dc.contributor.funder | Fundación Ramón Areces | - |
dc.identifier.funder | http://dx.doi.org/10.13039/100008054 | es_ES |
dc.identifier.pmid | 17913744 | - |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.openairetype | artículo | - |
item.grantfulltext | open | - |
item.cerifentitytype | Publications | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.fulltext | With Fulltext | - |
item.languageiso639-1 | en | - |
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