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http://hdl.handle.net/10261/37848
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dc.contributor.author | Pérez-Lago, Laura | - |
dc.contributor.author | Serrano-Heras, Gemma | - |
dc.contributor.author | Baños, Benito | - |
dc.contributor.author | Lázaro, José M. | - |
dc.contributor.author | Alcorlo, Martín | - |
dc.contributor.author | Villar, Laurentino | - |
dc.contributor.author | Salas, Margarita | - |
dc.date.accessioned | 2011-07-19T11:32:21Z | - |
dc.date.available | 2011-07-19T11:32:21Z | - |
dc.date.issued | 2011-05-12 | - |
dc.identifier.citation | Molecular Microbiology 80(6): 1657-1666 (2011) | es_ES |
dc.identifier.uri | http://hdl.handle.net/10261/37848 | - |
dc.description.abstract | Uracil-DNA glycosylase (UDG) is a conserved DNA repair enzyme involved in uracil excision from DNA. Here, we report the biochemical characterization of UDG encoded by Bacillus subtilis, a model low G+C Gram-positive organism. The purified enzyme removes uracil preferentially from single-stranded DNA over double-stranded DNA, exhibiting higher preference for U:G than U:A mismatches. Furthermore, we have identified key amino acids necessary for B. subtilis UDG activity. Our results showed that Asp-65 and His-187 are catalytic residues involved in glycosidic bond cleavage, whereas Phe-78 would participate in DNA recognition. Recently, it has been reported that B. subtilis phage φ29 encodes an inhibitor of the UDG enzyme, named protein p56, whose role has been proposed to ensure an efficient viral DNA replication, preventing the deleterious effect caused by UDG when it eliminates uracils present in the φ29 genome. In this work, we also show that a φ29-related phage, GA-1, encodes a p56-like protein with UDG inhibition activity. In addition, mutagenesis analysis revealed that residue Phe-191 of B. subtilis UDG is critical for the interaction with φ29 and GA-1 p56 proteins, suggesting that both proteins have similar mechanism of inhibition. | es_ES |
dc.description.sponsorship | This work was supported by the Spanish Ministry of Science and Innovation Grants BFU2008-00215 and CONSOLIDER-INGENIO CSD2007-00015 to M.S., by the Autonomous Community of Madrid Grant P-MAT-0283-0505 to M.S., by a grant from Fundación Mutua Madrileña to M.S. and by an institutional grant from Fundación Ramón Areces to the Centro de Biología Molecular Severo Ochoa. L.P.-L. was recipient of a postdoctoral fellowship of the Autonomous Community of Madrid. | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | John Wiley & Sons | es_ES |
dc.rights | closedAccess | es_ES |
dc.title | Characterization of Bacillus subtilis uracil-DNA glycosylase and its inhibition by phage φ29 protein p56 | es_ES |
dc.type | artículo | es_ES |
dc.identifier.doi | 10.1111/j.1365-2958.2011.07675.x | - |
dc.description.peerreviewed | Peer reviewed | es_ES |
dc.relation.publisherversion | http://dx.doi.org/10.1111/j.1365-2958.2011.07675.x | es_ES |
dc.contributor.funder | Ministerio de Ciencia e Innovación (España) | - |
dc.contributor.funder | Comunidad de Madrid | - |
dc.contributor.funder | Fundación Mutua Madrileña | - |
dc.contributor.funder | Fundación Ramón Areces | - |
dc.identifier.funder | http://dx.doi.org/10.13039/501100004837 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/100008061 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/100008054 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/100012818 | es_ES |
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 | No Fulltext | - |
item.cerifentitytype | Publications | - |
item.openairetype | artículo | - |
item.languageiso639-1 | en | - |
item.grantfulltext | none | - |
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