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Initial biochemical and functional characterization of a 5 `-nucleotidase from Xylella fastidiosa related to the human cytosolic 5 `-nucleotidase I

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Autor(es):
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Santos, Clelton A. [1] ; Saraiva, Antonio M. [1, 2] ; Toledo, Marcelo A. S. [1] ; Beloti, Lilian L. [1] ; Crucello, Aline [1] ; Favaro, Marianna T. P. [1] ; Horta, Maria A. C. [1] ; Santiago, Andre S. [1] ; Mendes, Juliano S. [1] ; Souza, Alessandra A. [3] ; Souza, Anete P. [1, 4]
Número total de Autores: 11
Afiliação do(s) autor(es):
[1] Univ Estadual Campinas, Ctr Biol Mol & Engn Genet, BR-13083875 Campinas, SP - Brazil
[2] Inst Nacl Metrol Qualidade & Tecnol, Rio De Janeiro, RJ - Brazil
[3] IAC, Ctr APTA Citros Sylvio Moreira, Cordeiropolis, SP - Brazil
[4] Univ Estadual Campinas, Inst Biol, Dept Biol Vegetal, BR-13083875 Campinas, SP - Brazil
Número total de Afiliações: 4
Tipo de documento: Artigo Científico
Fonte: Microbial Pathogenesis; v. 59-60, p. 1-6, JUN-JUL 2013.
Citações Web of Science: 5
Resumo

The 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. (C) 2013 Elsevier Ltd. All rights reserved. (AU)

Processo FAPESP: 01/07533-7 - Resolução da estrutura tridimensional de proteínas relacionadas à patogenicidade de Xyllela fastidiosa
Beneficiário:Anete Pereira de Souza
Linha de fomento: Auxílio à Pesquisa - Regular
Processo FAPESP: 08/55690-3 - Expressão, purificação e caracterização estrutural e funcional de proteínas relacionadas à patogenicidade de Xylella fastidiosa
Beneficiário:Clelton Aparecido dos Santos
Linha de fomento: Bolsas no Brasil - Doutorado