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dc.contributor.authorRomero, Patriciaes_ES
dc.contributor.authorLópez, Rubenses_ES
dc.contributor.authorGarcía, Ernestoes_ES
dc.date.accessioned2020-07-17T12:37:14Z-
dc.date.available2020-07-17T12:37:14Z-
dc.date.issued2004-12-
dc.identifier.citationJ Bacteriol 186(24) 8229-39 (2004)es_ES
dc.identifier.issn0021-9193-
dc.identifier.urihttp://hdl.handle.net/10261/216821-
dc.description11 p.-6 fig.-1 tab.es_ES
dc.description.abstractTwo new temperate bacteriophages exhibiting a Myoviridae (phiB6) and a Siphoviridae (phiHER) morphology have been isolated from Streptococcus mitis strains B6 and HER 1055, respectively, and partially characterized. The lytic phage genes were overexpressed in Escherichia coli, and their encoded proteins were purified. The lytAHER and lytAB6 genes are very similar (87% identity) and appeared to belong to the group of the so-called typical LytA amidases (atypical LytA displays a characteristic two-amino-acid deletion signature). although they exhibited several differential biochemical properties with respect to the pneumococcal LytA, e.g., they were inhibited in vitro by sodium deoxycholate and showed a more acidic pH for optimal activity. However, and in sharp contrast with the pneumococcal LytA, a short dialysis of LytAHER or LytAB6 resulted in reversible deconversion to the low-activity state (E-form) of the fully active phage amidases (C-form). Comparison of the amino acid sequences of LytAHER and LytAB6 with that of the pneumococcal amidase suggested that Val317 might be responsible for at least some of the peculiar properties of S. mitis phage enzymes. Site-directed mutagenesis that changed Val317 in the pneumococcal LytA amidase to a Thr residue (characteristic of LytAB6 and LytAHER) produced a fully active pneumococcal enzyme that differs from the parental one only in that the mutant amidase can reversibly recover the low-activity E-form upon dialysis. This is the first report showing that a single amino acid residue is involved in the conversion process of the major S. pneumoniae autolysin. Our results also showed that some lysogenic S. mitis strains possess a lytA-like gene, something that was previously thought to be exclusive to Streptococcus pneumoniae. Moreover, the newly discovered phage lysins constitute a missing link between the typical and atypical pneumococcal amidases known previously.es_ES
dc.description.sponsorshipThis work was supported by grants from the Dirección General de Investigación Científica y Técnica (BCM2003-00074) and from Redes Temáticas de Investigación Cooperativa (G03/103 and C03/14) (Ministerio de Sanidad y Consumo).es_ES
dc.language.isoenges_ES
dc.publisherAmerican Society for Microbiologyes_ES
dc.rightsclosedAccesses_ES
dc.subjectCell wallses_ES
dc.subjectTemperate bacteriophagees_ES
dc.subjectEscherichia-colies_ES
dc.subjectTeichoic acides_ES
dc.subjectMolecular characterizationes_ES
dc.subjectPneumoniaees_ES
dc.subjectGenees_ES
dc.subjectEnzymees_ES
dc.subjectCholinees_ES
dc.subjectIdentificationes_ES
dc.titleCharacterization of LytA-like N-acetylmuramoyl-L-alanine amidases from two new Streptococcus mitis bacteriophages provides insights into the properties of the major pneumococcal autolysines_ES
dc.typeartículoes_ES
dc.identifier.doi10.1128/JB.186.24.8229-8239.2004-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttps://doi.org/10.1128/JB.186.24.8229-8239.2004es_ES
dc.identifier.e-issn1098-5530-
dc.contributor.funderDirección General de Investigación Científica y Técnica, DGICT (España)es_ES
dc.contributor.funderMinisterio de Sanidad y Consumo (España)es_ES
dc.relation.csices_ES
oprm.item.hasRevisionno ko 0 false*
dc.identifier.funderhttp://dx.doi.org/10.13039/501100008737es_ES
dc.contributor.orcidGarcía, Ernesto [0000-0002-1741-5486]es_ES
dc.identifier.pmid15576771-
item.fulltextNo Fulltext-
item.openairetypeartículo-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.grantfulltextnone-
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