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http://dspace.mediu.edu.my:8181/xmlui/handle/10261/4821Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor | Ministerio de Educación y Ciencia (España) | - |
| dc.contributor | Fundación Ramón Areces | - |
| dc.creator | Longás, Elisa | - |
| dc.creator | Vega, Miguel de | - |
| dc.creator | Lázaro, José M. | - |
| dc.creator | Salas, Margarita | - |
| dc.date | 2008-06-05T13:50:22Z | - |
| dc.date | 2008-06-05T13:50:22Z | - |
| dc.date | 2006-10-28 | - |
| dc.date.accessioned | 2017-01-31T01:34:50Z | - |
| dc.date.available | 2017-01-31T01:34:50Z | - |
| dc.identifier | Nucleic Acids Research, 2006, Vol. 34, No. 20 6051–6063 | - |
| dc.identifier | 0305-1048 (Print) | - |
| dc.identifier | 1362-4962 (Online) | - |
| dc.identifier | http://hdl.handle.net/10261/4821 | - |
| dc.identifier.uri | http://dspace.mediu.edu.my:8181/xmlui/handle/10261/4821 | - |
| dc.description | PMCID: PMC1635332 Article available at http://dx.doi.org/10.1093/nar/gkl769 | - |
| dc.description | This paper shows that the protein-primed DNA polymerases encoded by bacteriophages Nf and GA-1, unlike other DNA polymerases, do not require unwinding or processivity factors for efficient synthesis of full-length terminal protein (TP)-DNA. Analysis of their polymerization activity shows that both DNA polymerases base their replication efficiency on a high processivity and on the capacity to couple polymerization to strand displacement. Both enzymes are endowed with a proofreading activity that acts coordinately with the polymerization one to edit polymerization errors. Additionally, Nf double-stranded DNA binding protein (DBP) greatly stimulated the in vitro formation of the TP-dAMP initiation complex by decreasing the Km value for dATP of the Nf DNA polymerase by >20-fold. Whereas Nf DNA polymerase, as the 29 enzyme, is able to use its homologous TP as well as DNA as primer, GA-1 DNA polymerase appears to have evolved to use its corresponding TP as the only primer of DNA synthesis. Such exceptional behaviour is discussed in the light of the recently solved structure of the DNA polymerase/TP complex of the related bacteriophage 29 | - |
| dc.description | This investigation was aided by research grant BFU 2005-00733 from the Spanish Ministry of Education and Science and by an institutional grant from Fundación Ramón Areces to the Centro de Biología Molecular ‘Severo Ochoa’. E.L. was a pre-doctoral fellow of the Ministerio de Educación y Ciencia. Funding to pay the Open Access publication charges for this article was provided by research grant BFU 2005-00733 from the Spanish Ministry of Education and Science. | - |
| dc.description | Peer reviewed | - |
| dc.format | 624384 bytes | - |
| dc.format | application/pdf | - |
| dc.language | eng | - |
| dc.publisher | Oxford University Press | - |
| dc.rights | openAccess | - |
| dc.subject | Bacteriophage Ф29 | - |
| dc.subject | DNA polymerases | - |
| dc.title | Functional characterization of highly processive protein-primed DNA polymerases from phages Nf and GA-1, endowed with a potent strand displacement capacity | - |
| dc.type | Artículo | - |
| Appears in Collections: | Digital Csic | |
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