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A putative twin-arginine translocation system in the phytopathogenic bacterium Xylella fastidiosa
  • Univ Lille 1
  • Universidade Estadual Paulista (UNESP)
  • Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
  • Centre national de la recherche scientifique (CNRS)
Sponsorship Process Number: 
  • CAPES: 370/01
  • CNRS: UMR 8576
The twin-arginine translocation (Tat) pathway of the xylem-limited phytopathogenic bacterium Xylella fastidiosa strain 9a5c, responsible for citrus variegated chlorosis, was explored. The presence of tatA, tatB, and tatC in the X. fastidiosa genome together with a list of proteins harboring 2 consecutive arginines in their signal peptides suggested the presence of a Tat pathway. The functional Tat dependence of X. fastidiosa OpgD was examined. Native or mutated signal peptides were fused to the beta-lactamase. Expression of fusion with intact signal peptides mediated high resistance to ampicillin in Escherichia coli tat(+) but not in the E. coli tat null mutant. The replacement of the 2 arginines by 2 lysines prevented the export of b-lactamase in E. coli tat(+), demonstrating that X. fastidiosa OpgD carries a signal peptide capable of engaging the E. coli Tat machinery. RT-PCR analysis revealed that the tat genes are transcribed as a single operon. tatA, tatB, and tatC genes were cloned. Complementation assays in E. coli devoid of all Tat or TatC components were unsuccessful, whereas X. fastidiosa Tat components led to a functional Tat translocase in E. coli TatB-deficient strain. Additional experiments implicated that X. fastidiosa TatB component could form a functional heterologous complex with the E. coli TatC component.
Issue Date: 
Canadian Journal of Microbiology. Ottawa: Canadian Science Publishing, Nrc Research Press, v. 57, n. 2, p. 149-154, 2011.
Time Duration: 
Canadian Science Publishing, Nrc Research Press
  • twin-arginine
  • Tat transport
  • Xylella fastidiosa
Access Rights: 
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Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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