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dc.typeArtigo de periódicopt_BR
dc.titleInitial Biochemical And Functional Characterization Of A 5'-nucleotidase From Xylella Fastidiosa Related To The Human Cytosolic 5'-nucleotidase I.pt_BR
dc.contributor.authorSantos, Clelton Apt_BR
dc.contributor.authorSaraiva, Antonio Mpt_BR
dc.contributor.authorToledo, Marcelo A Spt_BR
dc.contributor.authorBeloti, Lilian Lpt_BR
dc.contributor.authorCrucello, Alinept_BR
dc.contributor.authorFavaro, Marianna T Ppt_BR
dc.contributor.authorHorta, Maria A Cpt_BR
dc.contributor.authorSantiago, André Spt_BR
dc.contributor.authorMendes, Juliano Spt_BR
dc.contributor.authorSouza, Alessandra Apt_BR
dc.contributor.authorSouza, Anete Ppt_BR
unicamp.authorClelton A Santos, Centro de Biologia Molecular e Engenharia Genética, Universidade Estadual de Campinas, Campinas, SP, Brazil.pt_BR M Saraiva,pt A S Toledo,pt L Beloti,pt Crucello,pt T P Favaro,pt A C Horta,pté S Santiago,pt S Mendes,pt A Souza,pt P Souza,pt
dc.subjectGene Expression Profilingpt_BR
dc.subjectPhosphoric Monoester Hydrolasespt_BR
dc.subjectRecombinant Proteinspt_BR
dc.description.abstractThe 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.en
dc.relation.ispartofMicrobial Pathogenesispt_BR
dc.relation.ispartofabbreviationMicrob. Pathog.pt_BR
dc.identifier.citationMicrobial Pathogenesis. v. 59-60, p. 1-6pt_BR
dc.rights.holderCopyright © 2013 Elsevier Ltd. All rights reserved.pt_BR
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