کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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6136278 | 1593724 | 2013 | 6 صفحه PDF | دانلود رایگان |
The 5â²-nucleotidases constitute a ubiquitous family of enzymes that catalyze either the hydrolysis or the transfer of esterified phosphate at the 5â² 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 5â²-nucleotidase from Xylella fastidiosa that is related to the human cytosolic 5â²-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 Xf5â²-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 Xf5â²-Nt, we observed an overexpression of Xf5â²-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 5â²-nucleotidases may play an important role in bacterial biofilm formation, thereby contributing novel insights into bacterial nucleotide metabolism and pathogenicity.
⺠We report the characterization of a recombinant 5â²-nucleotidase from Xylella fastidiosa. ⺠X. fastidiosa Xf5â²-Nt is related to human cN-I. ⺠Xf5â²-Nt presents classical Michaelis-Menten behavior with pNPP as a substrate. ⺠Xf5â²-Nt is overexpressed in the initial phases of X. fastidiosa biofilm formation. ⺠De/phosphorylation network may play a key role in bacterial biofilm formation.
Journal: Microbial Pathogenesis - Volumes 59â60, JuneâJuly 2013, Pages 1-6