dc.creatorSantos, Clelton A
dc.creatorSaraiva, Antonio M
dc.creatorToledo, Marcelo A S
dc.creatorBeloti, Lilian L
dc.creatorCrucello, Aline
dc.creatorFavaro, Marianna T P
dc.creatorHorta, Maria A C
dc.creatorSantiago, André S
dc.creatorMendes, Juliano S
dc.creatorSouza, Alessandra A
dc.creatorSouza, Anete P
dc.date
dc.date2015-11-27T13:31:28Z
dc.date2015-11-27T13:31:28Z
dc.date.accessioned2018-03-29T01:17:20Z
dc.date.available2018-03-29T01:17:20Z
dc.identifierMicrobial Pathogenesis. v. 59-60, p. 1-6
dc.identifier1096-1208
dc.identifier10.1016/j.micpath.2013.02.007
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/23474016
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/200520
dc.identifier23474016
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1300753
dc.descriptionThe 5'-nucleotidases constitute a ubiquitous family of enzymes that catalyze either the hydrolysis or the transfer of esterified phosphate at the 5' position of nucleoside monophosphates. These enzymes are responsible for the regulation of nucleotide and nucleoside levels in the cell and can interfere with the phosphorylation-dependent activation of nucleoside analogs used in therapies targeting solid tumors and viral infections. In the present study, we report the initial biochemical and functional characterization of a 5'-nucleotidase from Xylella fastidiosa that is related to the human cytosolic 5'-nucleotidase I. X. fastidiosa is a plant pathogenic bacterium that is responsible for numerous economically important crop diseases. Biochemical assays confirmed the phosphatase activity of the recombinant purified enzyme and revealed metal ion dependence for full enzyme activity. In addition, we investigated the involvement of Xf5'-Nt in the formation of X. fastidiosa biofilms, which are structures that occlude the xylem vessels of susceptible plants and are strictly associated with bacterial pathogenesis. Using polyclonal antibodies against Xf5'-Nt, we observed an overexpression of Xf5'-Nt during the initial phases of X. fastidiosa biofilm formation that was not observed during X. fastidiosa planktonic growth. Our results demonstrate that the de/phosphorylation network catalyzed by 5'-nucleotidases may play an important role in bacterial biofilm formation, thereby contributing novel insights into bacterial nucleotide metabolism and pathogenicity.
dc.description59-60
dc.description1-6
dc.languageeng
dc.relationMicrobial Pathogenesis
dc.relationMicrob. Pathog.
dc.rightsfechado
dc.rightsCopyright © 2013 Elsevier Ltd. All rights reserved.
dc.sourcePubMed
dc.subject5'-nucleotidase
dc.subjectBiofilms
dc.subjectCoenzymes
dc.subjectGene Expression Profiling
dc.subjectMetals
dc.subjectPhosphoric Monoester Hydrolases
dc.subjectRecombinant Proteins
dc.subjectXylella
dc.titleInitial Biochemical And Functional Characterization Of A 5'-nucleotidase From Xylella Fastidiosa Related To The Human Cytosolic 5'-nucleotidase I.
dc.typeArtículos de revistas


Este ítem pertenece a la siguiente institución