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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | MULINARI, F. | |
dc.contributor.author | BECKER-RITT, A. B. | |
dc.contributor.author | DEMARTINI, D. R. | |
dc.contributor.author | LIGABUE-BRAUN, R. | |
dc.contributor.author | STANISÇUASKI, F. | |
dc.contributor.author | VERLI, H. | |
dc.contributor.author | FRAGOSO, R. R. | |
dc.contributor.author | SCHROEDER, E. K. | |
dc.contributor.author | CARLINI, C. R. | |
dc.contributor.author | GROSSI-de-SÁ, M. F. | |
dc.date.accessioned | 2018-09-27T00:34:36Z | - |
dc.date.available | 2018-09-27T00:34:36Z | - |
dc.date.created | 2012-01-23 | |
dc.date.issued | 2011 | |
dc.identifier.citation | Biochimica et Biophysica Acta, v. 1814, n. 12, p. 1758-1768, Dec. 2011. | |
dc.identifier.uri | http://www.alice.cnptia.embrapa.br/alice/handle/doc/913253 | - |
dc.description | Ureases, 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.iso | eng | eng |
dc.rights | openAccess | eng |
dc.title | Characterization of JBURE-IIb isoform of Canavalia ensiformis (L.) DC urease. | |
dc.type | Artigo de periódico | |
dc.date.updated | 2018-09-27T00:34:36Z | pt_BR |
dc.subject.thesagro | Canavalia Ensiformis | |
riaa.ainfo.id | 913253 | |
riaa.ainfo.lastupdate | 2018-09-26 | |
dc.contributor.institution | FERNANDA 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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