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| 1. |  | EMYGDIO, B. M.; PORTO, M. P; TEIXEIRA, M. C.; KONFLANZ, V.; MEIRELLES, W. F.; SILVA, S. D. dos A. e.; ACOSTA, A. Unidades Demonstrativas e de Observação de híbridos de milho na região de clima temperado - safra 2007/08. In: REUNIÃO TÉCNICA ANUAL DE MILHO, 53., REUNIÃO TÉCNICA ANUAL DE SORGO, 36., 2008. Pelotas. Atas e resumos... Pelotas: Embrapa Clima Temperado, 2008. 1 CD-ROM.| Biblioteca(s): Embrapa Clima Temperado. |
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| 2. | | EMYGDIO, B. M.; PORTO, M. P.; TEIXEIRA, M. C.; KONFLANZ, V.; MEIRELLES, W. F.; PEREIRA, F. R.; ACOSTA, A.; MACHADO, J. R. A.; HESS, J.; RIGO, F. Unidades demontrativas e de observação de híbridos de milho na região de clima temperado - safra 2008/09. In: REUNIÃO TÉCNICA ANUAL DO MILHO, 54.; REUNIÃO TÉCNICA ANUAL DO SORGO, 37., 2009, Pelotas. Atas e Resumos...Veranópolis: FEPAGRO, 2009. 1 CD-ROM.| Biblioteca(s): Embrapa Clima Temperado. |
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| 3. | | EMYGDIO, B. M.; SILVA, S. D. dos A. e.; PORTO, M. P; ACOSTA, A.; TEIXEIRA, M. C. KONFLANZ, V.; ÁVILA, T. T.; SILVA, A. V. SILVA, R. P. Unidades de observação de híbridos de milho na região de clima temperado - safra 2006/07. In: REUNIÃO TÉCNICA ANUAL DE MILHO, 52., REUNIÃO TÉCNICA ANUAL DE SORGO, 35., 2007. Santo Angelo. Atas e resumos... Pelotas: Embrapa Clima Temperado, 2008. 1 CD-ROM.| Biblioteca(s): Embrapa Clima Temperado. |
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| Registros recuperados : 3 | |
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Registro Completo
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Biblioteca(s): |
Embrapa Recursos Genéticos e Biotecnologia. |
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Data corrente: |
23/01/2012 |
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Data da última atualização: |
24/02/2023 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
A - 2 |
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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. |
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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. |
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Título: |
Characterization of JBURE-IIb isoform of Canavalia ensiformis (L.) DC urease. |
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Ano de publicação: |
2011 |
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Fonte/Imprenta: |
Biochimica et Biophysica Acta, v. 1814, n. 12, p. 1758-1768, Dec. 2011. |
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Idioma: |
Inglês |
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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. |
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Thesagro: |
Canavalia Ensiformis. |
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Categoria do assunto: |
-- |
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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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