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http://purl.uniprot.org/citations/24205926http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24205926http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24205926http://www.w3.org/2000/01/rdf-schema#comment"Protein-primed DNA replication constitutes a strategy to initiate viral DNA synthesis in a variety of prokaryotic and eukaryotic organisms. Although the main function of viral terminal proteins (TPs) is to provide a free hydroxyl group to start initiation of DNA replication, there are compelling evidences that TPs can also play other biological roles. In the case of Bacillus subtilis bacteriophage ϕ29, the N-terminal domain of the TP organizes viral DNA replication at the bacterial nucleoid being essential for an efficient phage DNA replication, and it contains a nuclear localization signal (NLS) that is functional in eukaryotes. Here we provide information about the structural properties of the ϕ29 TP N-terminal domain, which possesses sequence-independent DNA-binding capacity, and dissect the amino acid residues important for its biological function. By mutating all the basic residues of the TP N-terminal domain we identify the amino acids responsible for its interaction with the B. subtilis genome, establishing a correlation between the capacity of DNA-binding and nucleoid localization of the protein. Significantly, these residues are important to recruit the DNA polymerase at the bacterial nucleoid and, subsequently, for an efficient phage DNA replication."xsd:string
http://purl.uniprot.org/citations/24205926http://purl.org/dc/terms/identifier"doi:10.1111/mmi.12456"xsd:string
http://purl.uniprot.org/citations/24205926http://purl.org/dc/terms/identifier"doi:10.1111/mmi.12456"xsd:string
http://purl.uniprot.org/citations/24205926http://purl.uniprot.org/core/author"Salas M."xsd:string
http://purl.uniprot.org/citations/24205926http://purl.uniprot.org/core/author"Salas M."xsd:string
http://purl.uniprot.org/citations/24205926http://purl.uniprot.org/core/author"Redrejo-Rodriguez M."xsd:string
http://purl.uniprot.org/citations/24205926http://purl.uniprot.org/core/author"Redrejo-Rodriguez M."xsd:string
http://purl.uniprot.org/citations/24205926http://purl.uniprot.org/core/author"Holguera I."xsd:string
http://purl.uniprot.org/citations/24205926http://purl.uniprot.org/core/author"Holguera I."xsd:string
http://purl.uniprot.org/citations/24205926http://purl.uniprot.org/core/author"Munoz-Espin D."xsd:string
http://purl.uniprot.org/citations/24205926http://purl.uniprot.org/core/author"Munoz-Espin D."xsd:string
http://purl.uniprot.org/citations/24205926http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24205926http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24205926http://purl.uniprot.org/core/name"Mol. Microbiol."xsd:string
http://purl.uniprot.org/citations/24205926http://purl.uniprot.org/core/name"Mol. Microbiol."xsd:string
http://purl.uniprot.org/citations/24205926http://purl.uniprot.org/core/pages"232-241"xsd:string
http://purl.uniprot.org/citations/24205926http://purl.uniprot.org/core/pages"232-241"xsd:string
http://purl.uniprot.org/citations/24205926http://purl.uniprot.org/core/title"New insights in the Phi29 terminal protein DNA-binding and host nucleoid localization functions."xsd:string
http://purl.uniprot.org/citations/24205926http://purl.uniprot.org/core/title"New insights in the Phi29 terminal protein DNA-binding and host nucleoid localization functions."xsd:string
http://purl.uniprot.org/citations/24205926http://purl.uniprot.org/core/volume"91"xsd:string
http://purl.uniprot.org/citations/24205926http://purl.uniprot.org/core/volume"91"xsd:string
http://purl.uniprot.org/citations/24205926http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24205926
http://purl.uniprot.org/citations/24205926http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24205926