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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Serrano-Heras, Gemma | - |
dc.contributor.author | Ruiz-Masó, José A. | - |
dc.contributor.author | Solar, Gloria del | - |
dc.contributor.author | Espinosa, Manuel | - |
dc.contributor.author | Bravo, Alicia | - |
dc.contributor.author | Salas, Margarita | - |
dc.date.accessioned | 2008-10-20T14:28:17Z | - |
dc.date.available | 2008-10-20T14:28:17Z | - |
dc.date.issued | 2007-08-13 | - |
dc.identifier.citation | Nucleic Acids Research 35(16):5393-5401 (2007) | en_US |
dc.identifier.issn | 0305-1048 | - |
dc.identifier.uri | http://hdl.handle.net/10261/7897 | - |
dc.description.abstract | Protein p56 (56 amino acids) from the Bacillus subtilis phage phi 29 inactivates the host uracil-DNA glycosylase (UDG), an enzyme involved in the base excision repair pathway. At present, p56 is the only known example of a UDG inhibitor encoded by a non-uracil containing viral DNA. Using analytical ultracentrifugation methods, we found that protein p56 formed dimers at physiological concentrations. In addition, circular dichroism spectroscopic analyses revealed that protein p56 had a high content of ß-strands (around 40%). To understand the mechanism underlying UDG inhibition by p56, we carried out in vitro experiments using the Escherichia coli UDG enzyme. The highly acidic protein p56 was able to compete with DNA for binding to UDG. Moreover, the interaction between p56 and UDG blocked DNA binding by UDG. We also demonstrated that Ugi, a protein that interacts with the DNA-binding domain of UDG, was able to replace protein p56 previously bound to the UDG enzyme. These results suggest that protein p56 could be a novel naturally occurring DNA mimicry | en_US |
dc.description.sponsorship | This work was supported by grants BFU2005-00733/BMC (Ministerio de Educación y Ciencia) and S-0505/MAT-0283 (Comunidad Autónoma de Madrid) to M.S. and by grants BFU2004-00687/BMC (Ministerio de Educación y Ciencia) and S-BIO-02602006 (COMBACT) (Comunidad Autónoma de Madrid) to M.E. The institutional help of Fundación Ramón Areces to the Centro de Biología Molecular ‘Severo Ochoa’ is acknowledged. G.S.-H. had an I3P contract from the Spanish National Research Council. Funding to pay the Open Access publication charges for this article was provided by BFU2005-00733/BMC from Spanish Ministry of Education and Science | en_US |
dc.format.extent | 1495744 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 | Bacillus subtilis | en_US |
dc.subject | Phage phi 29 | en_US |
dc.subject | Escherichia coli | en_US |
dc.title | Protein p56 from the Bacillus subtilis phage phi 29 inhibits DNA-binding ability of uracil-DNA glycosylase | en_US |
dc.type | artículo | en_US |
dc.identifier.doi | 10.1093/nar/gkm584 | - |
dc.description.peerreviewed | Peer reviewed | en_US |
dc.relation.publisherversion | http://dx.doi.org/10.1093/nar/gkm584 | en_US |
dc.identifier.e-issn | 1362-4962 | - |
dc.contributor.funder | Ministerio de Educación y Ciencia (España) | - |
dc.contributor.funder | Comunidad de Madrid | - |
dc.contributor.funder | European Commission | - |
dc.identifier.funder | http://dx.doi.org/10.13039/501100000780 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/100012818 | es_ES |
dc.identifier.pmid | 17698500 | - |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.fulltext | With Fulltext | - |
item.cerifentitytype | Publications | - |
item.openairetype | artículo | - |
item.languageiso639-1 | en | - |
item.grantfulltext | open | - |
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