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http://hdl.handle.net/10662/7087
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Campo DC | Valor | idioma |
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dc.contributor.author | López Villamizar, Iralis Mercedes | - |
dc.contributor.author | Cabezas Martín, Alicia | - |
dc.contributor.author | Pinto Corraliza, Rosa María | - |
dc.contributor.author | Canales García, José | - |
dc.contributor.author | Ribeiro, João Nuno Meireles da Silva Gonçalves | - |
dc.contributor.author | Cameselle Viña, José Carlos | - |
dc.contributor.author | Costas Vázquez, María Jesús | - |
dc.date.accessioned | 2018-03-06T09:41:36Z | - |
dc.date.available | 2018-03-06T09:41:36Z | - |
dc.date.issued | 2016 | - |
dc.identifier.issn | 1932-6203 | - |
dc.identifier.uri | http://hdl.handle.net/10662/7087 | - |
dc.description.abstract | Endogenous cyclic diadenylate phosphodiesterase activity was accidentally detected in lysates of Escherichia coli BL21. Since this kind of activity is uncommon in Gram-negative bacteria, its identification was undertaken. After partial purification and analysis by denaturing gel electrophoresis, renatured activity correlated with a protein identified by fingerprinting as CpdB (cpdB gene product), which is annotated as 3´-nucleotidase / 2´,3´- cyclicmononucleotide phosphodiesterase, and it is synthesized as a precursor protein with a signal sequence removable upon export to the periplasm. It has never been studied as a recombinant protein. The coding sequence of mature CpdB was cloned and expressed as a GST fusion protein. The study of the purified recombinant protein, separated from GST, confirmed CpdB annotation. The assay of catalytic efficiencies (kcat/Km) for a large substrate set revealed novel CpdB features, including very high efficiencies for 3´-AMP and 2´,3´- cyclic mononucleotides, and previously unknown activities on cyclic and linear dinucleotides. The catalytic efficiencies of the latter activities, though low in relative terms when compared to the major ones, are far from negligible. Actually, they are perfectly comparable to those of the ‘average’ enzyme and the known, bona fide cyclic dinucleotide phosphodiesterases. On the other hand, CpdB differs from these enzymes in its extracytoplasmic location and in the absence of EAL, HD and DHH domains. Instead, it contains the domains of the 5´-nucleotidase family pertaining to the metallophosphoesterase superfamily, although CpdB lacks 5´-nucleotidase activity. The possibility that the extracytoplasmic activity of CpdB on cyclic dinucleotides could have physiological meaning is discussed. | es_ES |
dc.description.sponsorship | Trabajo financiado por: Junta de Extremadura y Fondos FEDER. Ayudas GR10133 y GR15143 Donación privada para María Jesús Costas Vázquez. Contrato 2015/00481/001 | es_ES |
dc.format.extent | 22 p. | es_ES |
dc.format.mimetype | application/pdf | en_US |
dc.language.iso | eng | es_ES |
dc.publisher | Public Library of Science | es_ES |
dc.rights | Atribución-NoComercial-SinDerivadas 3.0 España | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/3.0/es/ | * |
dc.subject | Escherichia coli BL21 | es_ES |
dc.subject | Bacteria Gram-Negativo | es_ES |
dc.subject | Proteina fusión con GST | es_ES |
dc.subject | Electroforesis de proteinas desnaturalizantes | es_ES |
dc.subject | Gram-negative bacteria | es_ES |
dc.subject | GST fusion protein | es_ES |
dc.subject | Denaturing gel electrophoresis | es_ES |
dc.title | The characterization of Escherichia coli CpdB as a recombinantpProtein reveals that, besides having the expected 3´-nucleotidase and 2´,3´-cyclic mononucleotide phosphodiesterase activities, it is also active as cyclic dinucleotide phosphodiesterase | es_ES |
dc.type | article | es_ES |
dc.description.version | peerReviewed | es_ES |
europeana.type | TEXT | en_US |
dc.rights.accessRights | openAccess | es_ES |
dc.subject.unesco | 2302.27 Proteínas | es_ES |
dc.subject.unesco | 2414.02 Fisiología Bacteriana | es_ES |
europeana.dataProvider | Universidad de Extremadura. España | es_ES |
dc.identifier.bibliographicCitation | López Villamizar, I.; Cabezas Martín, A.; Pinto Corraliza, R. M.; Canales García, J.; Ribeiro, J. N. Meireles da Silva Gonçalves; Cameselle Viña, J. C. y Costas Vázquez, M. J. (2016). The characterization of Escherichia coli CpdB as a recombinantpProtein reveals that, besides having the expected 3´-nucleotidase and 2´,3´-cyclic mononucleotide phosphodiesterase activities, it is also active as cyclic dinucleotide phosphodiesterase. PLoS ONE, 11, 6, e0157308. ESSN 1932-6203 | es_ES |
dc.type.version | publishedVersion | es_ES |
dc.contributor.affiliation | Universidad de Extremadura. Departamento de Bioquímica, Biología Molecular y Genética | es_ES |
dc.relation.publisherversion | http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0157308 | es_ES |
dc.identifier.doi | 10.1371/journal.pone.0157308 | - |
dc.identifier.publicationtitle | PLoS ONE | es_ES |
dc.identifier.publicationissue | 6 | es_ES |
dc.identifier.publicationfirstpage | 1 | es_ES |
dc.identifier.publicationlastpage | 22 | es_ES |
dc.identifier.publicationvolume | 11, e015308 | es_ES |
Colección: | DBYBM - Artículos |
Archivos
Archivo | Descripción | Tamaño | Formato | |
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journal_pone_0157308.PDF | 1,62 MB | Adobe PDF | Descargar |
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