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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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Embrapa Cerrados (CPAC) |
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| 1. |  | AGATA, K.; ALASAAD, S.; ALMEIDA-VAL, V. M. F.; ÁLVAREZ-DIOS, J. A.; BARBISAN, F.; BEADELL, J. S.; BELTRÁN, J. F.; BENÍTEZ, M.; BINO, G.; BLEAY, C.; BLOOR, P.; BOHLMANN, J.; BOOTH, W.; BOSCARI, E.; CACCONE, A.; CAMPOS, T. de; CARVALHO, B. M.; CLIMACO, G. T.; CLOBERT, J.; CONGIU, L.; COWGER, C.; DIAS, G.; DOADRIO, I.; FARIAS, I. P.; FERRAND, N.; FREITAS, P. D.; FUSCO, G.; GALETTI, P. M.; GALLARDO-ESCÁRATE, C.; GAUNT, M. W.; OCAMPO, Z. G.; GONÇALVES, H.; GONZALEZ, E. G.; HAYE, P.; HONNAY, O.; HYSENI, C.; JACQUEMYN, H.; JOWERS, M. J.; KAKEZAWA, A.; KAWAGUCHI, E.; KEELING, C. I.; YE-SEUL, K.; LA SPINA, M.; WAN-OK, L.; LESNIEWSKA, M.; YANG, L.; HAIXIA, L.; XIAOLIN, L.; LOPES, S.; MARTÍNEZ, P.; MEEUS, S.; MURRAY, B. W.; NUNES, A. G.; OKEDI, L. M.; OUMA, J. O.; PARDO, B. G.; PARKS, R.; PAULA-SILVA, M. N.; PEDRAZA-LARA, C.; PERERA, O. P.; PINO-QUERIDO, A.; RICHARD, M.; ROSSINI, B. C.; SAMARASEKERA, N. G.; SÁNCHEZ, A.; SANCHEZ, J. A.; SANTOS C. H. dos A.; SHINOHARA, W.; SORIGUER, R. C.; SOUSA, A. C. B.; SOUSA, C. F. da S.; STEVENS, V. M.; TEJEDO, M.; VALENZUELA-BUSTAMANTE, M.; VLIET, M. S. V. de; VANDEPITTE, K.; VERA, M.; WANDELER, P.; WEIMIN, W.; YONG-JIN, W.; YAMASHIRO, A.; YAMASHIRO, T.; CHANGCHENG, Z. Permanent genetic resources added to molecular ecology. Resources database 1 December 2010-31 January 2011. Molecular Ecology Resources, Oxford, v. 11, n. 3, p. 935-936, May 2011.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: B - 2 |
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