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dc.contributor.authorMULINARI, F.
dc.contributor.authorBECKER-RITT, A. B.
dc.contributor.authorDEMARTINI, D. R.
dc.contributor.authorLIGABUE-BRAUN, R.
dc.contributor.authorSTANISÇUASKI, F.
dc.contributor.authorVERLI, H.
dc.contributor.authorFRAGOSO, R. R.
dc.contributor.authorSCHROEDER, E. K.
dc.contributor.authorCARLINI, C. R.
dc.contributor.authorGROSSI-de-SÁ, M. F.
dc.date.accessioned2018-09-27T00:34:36Z-
dc.date.available2018-09-27T00:34:36Z-
dc.date.created2012-01-23
dc.date.issued2011
dc.identifier.citationBiochimica et Biophysica Acta, v. 1814, n. 12, p. 1758-1768, Dec. 2011.
dc.identifier.urihttp://www.alice.cnptia.embrapa.br/alice/handle/doc/913253-
dc.descriptionUreases, nickel-dependent enzymes that catalyze the hydrolysis of urea into ammonia and bicarbonate, are widespread in plants, bacteria, and fungi. Previously, we cloned a cDNA encoding a Canavalia ensiformis urease isoform named JBURE-II, corresponding to a putative smaller urease protein (78 kDa) when compared to other plant ureases. Aiming to produce the recombinant protein, we obtained jbure-IIb, with different 3? and 5? ends, encoding a 90 kDa urease. Three peptides unique to the JBURE-II/-IIb protein were detected by mass spectrometry in seed extracts, indicating that jbure-II/-IIb is a functional gene. Comparative modeling indicates that JBURE-IIb urease has an overall shape almost identical to C. ensiformis major urease JBURE-I with all residues critical for urease activity. The cDNA was cloned into the pET101 vector and the recombinant protein was produced in Escherichia coli. The JBURE-IIb protein, although enzymatically inactive presumably due to the absence of Ni atoms in its active site, impaired the growth of a phytopathogenic fungus and showed entomotoxic properties, inhibiting diuresis of Rhodnius prolixus isolated Malpighian tubules, in concentrations similar to those reported for JBURE-I and canatoxin. The antifungal and entomotoxic properties of the recombinant JBURE-IIb apourease are consistent with a protective role of ureases in plants.
dc.language.isoengeng
dc.rightsopenAccesseng
dc.titleCharacterization of JBURE-IIb isoform of Canavalia ensiformis (L.) DC urease.
dc.typeArtigo de periódico
dc.date.updated2018-09-27T00:34:36Zpt_BR
dc.subject.thesagroCanavalia Ensiformis
riaa.ainfo.id913253
riaa.ainfo.lastupdate2018-09-26
dc.contributor.institutionFERNANDA MULINARI, UFRGS; ARLETE BEATRIZ BECKER-RITT, UFRGS; DIOGO RIBEIRO DEMARTINI, UFRGS; RODRIGO LIGABUE-BRAUN, UFRGS; FERNANDA STANISÇUASKI, UFRGS; HUGO VERLI, UFRGS; RODRIGO DA ROCHA FRAGOSO, CPAC; EVELYN KOECHE SCHROEDER, UFRGS; CÉLIA REGINA CARLINI, UFRGS; MARIA FATIMA GROSSI DE SA, CENARGEN.
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