Characterization of JBURE-IIb isoform of Canavalia ensiformis (L.) DC urease.

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dc.contributorFERNANDA MULINARI, UNIVERSIDADE FEDERAL DO RIO GRANDE DO SUL
dc.contributorARLETE BEATRIZ BECKER-RITT, UNIVERSIDADE FEDERAL DO RIO GRANDE DO SUL
dc.contributorDIOGO RIBEIRO DEMARTINI, UNIVERSIDADE FEDERAL DO RIO GRANDE DO SUL
dc.contributorRODRIGO LIGABUE-BRAUN, UNIVERSIDADE FEDERAL DO RIO GRANDE DO SUL
dc.contributorFERNANDA STANISÇUASKI, UNIVERSIDADE FEDERAL DO RIO GRANDE DO SUL
dc.contributorHUGO VERLI, UNIVERSIDADE FEDERAL DO RIO GRANDE DO SUL
dc.contributorRODRIGO DA ROCHA FRAGOSO, CPAC
dc.contributorEVELYN KOECHE SCHROEDER, UNIVERSIDADE FEDERAL DO RIO GRANDE DO SUL
dc.contributorCÉLIA REGINA CARLINI, UNIVERSIDADE FEDERAL DO RIO GRANDE DO SUL
dc.contributorMARIA FATIMA GROSSI DE SA, CENARGEN.
dc.creatorMULINARI, F.
dc.creatorBECKER-RITT, A. B.
dc.creatorDEMARTINI, D. R.
dc.creatorLIGABUE-BRAUN, R.
dc.creatorSTANISÇUASKI, F.
dc.creatorVERLI, H.
dc.creatorFRAGOSO, R. R.
dc.creatorSCHROEDER, E. K.
dc.creatorCARLINI, C. R.
dc.creatorSA, M. F. G. de
dc.date2018-09-27T00:34:36Z
dc.date2018-09-27T00:34:36Z
dc.date2012-01-23
dc.date2011
dc.date2018-09-27T00:34:36Z
dc.date.accessioned2026-07-07T11:52:02Z
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.identifierBiochimica et Biophysica Acta, v. 1814, n. 12, p. 1758-1768, Dec. 2011.
dc.identifierhttp://www.alice.cnptia.embrapa.br/alice/handle/doc/913253
dc.identifier.urihttp://hdl.handle.net/123456789/515574
dc.languageeng
dc.rightsopenAccess
dc.subjectCanavalia Ensiformis
dc.titleCharacterization of JBURE-IIb isoform of Canavalia ensiformis (L.) DC urease.
dc.typeArtigo de periódico

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