A putative twin-arginine translocation system in the phytopathogenic bacterium Xylella fastidiosa

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorCiapina, Luciane Prioli
dc.creatorPicchi, Simone Cristina
dc.creatorLacroix, Jean-Marie
dc.creatorGertrudes de Macedo Lemos, Eliana
dc.creatorOedberg-Ferragut, Carmen
dc.date2014-05-20T15:32:02Z
dc.date2016-10-25T18:08:07Z
dc.date2014-05-20T15:32:02Z
dc.date2016-10-25T18:08:07Z
dc.date2011-02-01
dc.date.accessioned2017-04-06T00:25:30Z
dc.date.available2017-04-06T00:25:30Z
dc.identifierCanadian Journal of Microbiology. Ottawa: Canadian Science Publishing, Nrc Research Press, v. 57, n. 2, p. 149-154, 2011.
dc.identifier0008-4166
dc.identifierhttp://hdl.handle.net/11449/41035
dc.identifierhttp://acervodigital.unesp.br/handle/11449/41035
dc.identifier10.1139/W10-111
dc.identifierWOS:000287610300010
dc.identifierhttp://dx.doi.org/10.1139/W10-111
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/883762
dc.descriptionThe 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.
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.languageeng
dc.publisherCanadian Science Publishing, Nrc Research Press
dc.relationCanadian Journal of Microbiology
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjecttwin-arginine
dc.subjectTat transport
dc.subjectXylella fastidiosa
dc.titleA putative twin-arginine translocation system in the phytopathogenic bacterium Xylella fastidiosa
dc.typeOtro


Este ítem pertenece a la siguiente institución