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Registro Completo |
Biblioteca(s): |
Embrapa Recursos Genéticos e Biotecnologia. |
Data corrente: |
23/01/2012 |
Data da última atualização: |
24/02/2023 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Autoria: |
MULINARI, F.; BECKER-RITT, A. B.; DEMARTINI, D. R.; LIGABUE-BRAUN, R.; STANISÇUASKI, F.; VERLI, H.; FRAGOSO, R. R.; SCHROEDER, E. K.; CARLINI, C. R.; GROSSI-de-SÁ, M. F. |
Afiliação: |
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. |
Título: |
Characterization of JBURE-IIb isoform of Canavalia ensiformis (L.) DC urease. |
Ano de publicação: |
2011 |
Fonte/Imprenta: |
Biochimica et Biophysica Acta, v. 1814, n. 12, p. 1758-1768, Dec. 2011. |
Idioma: |
Inglês |
Conteúdo: |
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. |
Thesagro: |
Canavalia Ensiformis. |
Categoria do assunto: |
-- |
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/183508/1/1-s2.0-S1570963911002172-main.pdf
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Marc: |
LEADER 02105naa a2200241 a 4500 001 1913253 005 2023-02-24 008 2011 bl uuuu u00u1 u #d 100 1 $aMULINARI, F. 245 $aCharacterization of JBURE-IIb isoform of Canavalia ensiformis (L.) DC urease.$h[electronic resource] 260 $c2011 520 $aUreases, 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. 650 $aCanavalia Ensiformis 700 1 $aBECKER-RITT, A. B. 700 1 $aDEMARTINI, D. R. 700 1 $aLIGABUE-BRAUN, R. 700 1 $aSTANISÇUASKI, F. 700 1 $aVERLI, H. 700 1 $aFRAGOSO, R. R. 700 1 $aSCHROEDER, E. K. 700 1 $aCARLINI, C. R. 700 1 $aGROSSI-de-SÁ, M. F. 773 $tBiochimica et Biophysica Acta$gv. 1814, n. 12, p. 1758-1768, Dec. 2011.
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Embrapa Recursos Genéticos e Biotecnologia (CENARGEN) |
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1. | | SIMON, R. A.; KIIHL, T. A. M.; REGITANO NETO, A.; RAMOS, N. P.; LIMA, C. P.; FINOTO, E. L. Avaliação de cultivares de mamona em diferentes densidades de semeadura. In: CONGRESSO BRASILEIRO DE MELHORAMENTO DE PLANTAS, 6., 2011, Búzios. Panorama atual e perspectivas do melhoramento de plantas no Brasil. [Búzios]: SBMP, 2011. 1 CD-ROM.Tipo: Artigo em Anais de Congresso |
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