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Registro Completo |
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Biblioteca(s): |
Embrapa Cerrados. |
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Data corrente: |
22/12/2011 |
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Data da última atualização: |
22/12/2011 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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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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ISSN: |
1570-9639 |
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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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Marc: |
LEADER 02108naa a2200253 a 4500
001 1910728
005 2011-12-22
008 2011 bl --- 0-- u #d
022 $a1570-9639
100 1 $aMULINARI, F.
245 $aCharacterization of JBURE-IIb isoform of Canavalia ensiformis (L.) DC urease.
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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Registro original: |
Embrapa Cerrados (CPAC) |
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 | Acesso ao texto completo restrito à biblioteca da Embrapa Agrobiologia. Para informações adicionais entre em contato com cnpab.biblioteca@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Agrobiologia. |
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Data corrente: |
29/12/2016 |
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Data da última atualização: |
29/12/2016 |
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Tipo da produção científica: |
Resumo em Anais de Congresso |
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Autoria: |
HOFMANN, A.; FISHER, D.; ROUWS, L. F. M.; SCHWAB, S.; HARTMANN, A.; BALDANI, J. I. |
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Afiliação: |
ANDREAS HOFMANN, BOLSISTA EMBRAPA AGROBIOLOGIA; DOREEN FISHER, BOLSISTA EMBRAPA AGROBIOLOGIA; LUC FELICIANUS MARIE ROUWS, CNPAB; STEFAN SCHWAB, CNPAB; ANTON HARTMANN, GERMAN RESEARCH CENTER FOR ENVIRONMENTAL HEALTH; JOSE IVO BALDANI, CNPAB. |
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Título: |
Relevance of the Gluconacetobacter diazotrophicus PAL5 LUX/LUSR quorum sensing system for its plants growth promotion and plant microbe interaction. |
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Ano de publicação: |
2016 |
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Fonte/Imprenta: |
In: TALLER LATIONOAMERICANO DE PGPR, 3., 2016. Chile. Libro de Resúmenes. Pucón, CH: Universidad de La Frontera, 2016 |
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Idioma: |
Inglês |
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Palavras-Chave: |
Plant growt promotion. |
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Thesaurus NAL: |
Confocal laser scanning microscopy. |
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Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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Marc: |
LEADER 00707naa a2200193 a 4500
001 2059637
005 2016-12-29
008 2016 bl --- 0-- u #d
100 1 $aHOFMANN, A.
245 $aRelevance of the Gluconacetobacter diazotrophicus PAL5 LUX/LUSR quorum sensing system for its plants growth promotion and plant microbe interaction.
260 $c2016
650 $aConfocal laser scanning microscopy
653 $aPlant growt promotion
700 1 $aFISHER, D.
700 1 $aROUWS, L. F. M.
700 1 $aSCHWAB, S.
700 1 $aHARTMANN, A.
700 1 $aBALDANI, J. I.
773 $tIn: TALLER LATIONOAMERICANO DE PGPR, 3., 2016. Chile. Libro de Resúmenes. Pucón, CH: Universidad de La Frontera, 2016
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