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Registro Completo |
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Biblioteca(s): |
Embrapa Milho e Sorgo. |
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Data corrente: |
01/12/2009 |
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Data da última atualização: |
13/07/2018 |
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Tipo da produção científica: |
Artigo em Anais de Congresso / Nota Técnica |
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Autoria: |
HOEKENGA, O. A.; BUCKLER, E. S.; KIRST, M.; KRILL, A. M.; LYI, S. M.; MAGALHAES, J. V. de; MARON, L. G.; KOCHIAN, L. V. |
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Afiliação: |
Owen A. Hoekenga, Cornell University; E. S. Buchkler, University of Florida; M. Kirst, University of Florida; JURANDIR VIEIRA DE MAGALHAES, CNPMS. |
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Título: |
Joint linkage-association analysis of aluminum tolerance in maize. |
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Ano de publicação: |
2009 |
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Fonte/Imprenta: |
In: INTERNATIONAL SYMPOSIUM ON PLANT-SOIL INTERACTIONS AT LOW pH, 7., 2009, Guangzhou. Plant-soil interactions at low pH: nutriomic approach: proceedings. Guangzhou: South China University of Technology, 2009. p. 136-137. |
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Idioma: |
Inglês |
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Palavras-Chave: |
Tolerância ao alumínio. |
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Thesagro: |
Milho. |
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Categoria do assunto: |
S Ciências Biológicas |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/58107/1/Joint-linkage.pdf
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Marc: |
LEADER 00776nam a2200205 a 4500
001 1576798
005 2018-07-13
008 2009 bl uuuu u00u1 u #d
100 1 $aHOEKENGA, O. A.
245 $aJoint linkage-association analysis of aluminum tolerance in maize.$h[electronic resource]
260 $aIn: INTERNATIONAL SYMPOSIUM ON PLANT-SOIL INTERACTIONS AT LOW pH, 7., 2009, Guangzhou. Plant-soil interactions at low pH: nutriomic approach: proceedings. Guangzhou: South China University of Technology, 2009. p. 136-137.$c2009
650 $aMilho
653 $aTolerância ao alumínio
700 1 $aBUCKLER, E. S.
700 1 $aKIRST, M.
700 1 $aKRILL, A. M.
700 1 $aLYI, S. M.
700 1 $aMAGALHAES, J. V. de
700 1 $aMARON, L. G.
700 1 $aKOCHIAN, L. V.
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Registro original: |
Embrapa Milho e Sorgo (CNPMS) |
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Voltar
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Registro Completo
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Biblioteca(s): |
Embrapa Recursos Genéticos e Biotecnologia; Embrapa Soja. |
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Data corrente: |
01/03/2011 |
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Data da última atualização: |
14/02/2023 |
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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: |
VASCONCELOS, E. A. R.; SANTANA, C. G.; GODOY, C. V.; SEIXAS, C. D. S.; SILVA, M. S.; MOREIRA, L. R. S.; OLIVEIRA-NETO, O. B.; PRICE, D.; FITCHES, E.; FERREIRA FILHO, E. X.; MEHTA, A.; GATEHOUSE, J. A.; GROSSI-DE-SA, M. F. |
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Afiliação: |
ERICO A. R. VASCONCELOS, Embrapa Recursos Genéticos e Biotecnologia; CELSO G. SANTANA, Embrapa Recursos Genéticos e Biotecnologia; CLAUDIA VIEIRA GODOY, CNPSO; CLAUDINE DINALI SANTOS SEIXAS, CNPSO; MARILIA SANTOS SILVA, CPAC; LEONORA R. S. MOREIRA, UNB; OSMUNDO B. OLIVEIRA-NETO, Embrapa Recursos Genéticos e Biotecnologia; DANIEL PRICE, Durham University; ELAINE FITCHES, Durham University; EDIVALDO XIMENES FERREIRA FILHO, UNB; ANGELA MEHTA DOS REIS, CENARGEN; JOHN A. GATEHOUSE, Durham University; MARIA FATIMA GROSSI DE SA, CENARGEN. |
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Título: |
A new chitinase-like xylanase inhibitor protein (XIP) from coffee (Coffea arabica) affects Soybean Asian rust (Phakopsora pachyrhizi) spore germination. |
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Ano de publicação: |
2011 |
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Fonte/Imprenta: |
BMC Biotechnology, v. 11, 2011. |
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Idioma: |
Inglês |
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Notas: |
Disponível em:Acesso em: 1 mar. 2011. |
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Conteúdo: |
Background: Asian rust (Phakopsora pachyrhizi) is a common disease in Brazilian soybean fields and it is difficult to control. To identify a biochemical candidate with potential to combat this disease, a new chitinase-like xylanase inhibitor protein (XIP) from coffee (Coffea arabica) (CaclXIP) leaves was cloned into the pGAPZa-B vector for expression in Pichia pastoris. Results: A cDNA encoding a chitinase-like xylanase inhibitor protein (XIP) from coffee (Coffea arabica) (CaclXIP), was isolated from leaves. The amino acid sequence predicts a (b/a)8 topology common to Class III Chitinases (glycoside hydrolase family 18 proteins; GH18), and shares similarity with other GH18 members, although it lacks the glutamic acid residue essential for catalysis, which is replaced by glutamine. CaclXIP was expressed as a recombinant protein in Pichia pastoris. Enzymatic assay showed that purified recombinant CaclXIP had only residual chitinolytic activity. However, it inhibited xylanases from Acrophialophora nainiana by approx. 60% when present at 12:1 (w/w) enzyme:inhibitor ratio. Additionally, CaclXIP at 1.5 ?g/?L inhibited the germination of spores of Phakopsora pachyrhizi by 45%. Conclusions: Our data suggests that CaclXIP belongs to a class of naturally inactive chitinases that have evolved to act in plant cell defence as xylanase inhibitors. Its role on inhibiting germination of fungal spores makes it an eligible candidate gene for the control of Asian rust. |
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Thesagro: |
Doença de planta; Soja. |
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Thesaurus NAL: |
Plant diseases and disorders; Soybeans. |
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Categoria do assunto: |
F Plantas e Produtos de Origem Vegetal |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/28883/1/a-new-chitinase-like-xylanase-inhibitor.pdf
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Marc: |
LEADER 02499naa a2200325 a 4500
001 1901430
005 2023-02-14
008 2011 bl uuuu u00u1 u #d
100 1 $aVASCONCELOS, E. A. R.
245 $aA new chitinase-like xylanase inhibitor protein (XIP) from coffee (Coffea arabica) affects Soybean Asian rust (Phakopsora pachyrhizi) spore germination.
260 $c2011
500 $aDisponível em:<http://www.biomedcentral.com/1472-6750/11/14>Acesso em: 1 mar. 2011.
520 $aBackground: Asian rust (Phakopsora pachyrhizi) is a common disease in Brazilian soybean fields and it is difficult to control. To identify a biochemical candidate with potential to combat this disease, a new chitinase-like xylanase inhibitor protein (XIP) from coffee (Coffea arabica) (CaclXIP) leaves was cloned into the pGAPZa-B vector for expression in Pichia pastoris. Results: A cDNA encoding a chitinase-like xylanase inhibitor protein (XIP) from coffee (Coffea arabica) (CaclXIP), was isolated from leaves. The amino acid sequence predicts a (b/a)8 topology common to Class III Chitinases (glycoside hydrolase family 18 proteins; GH18), and shares similarity with other GH18 members, although it lacks the glutamic acid residue essential for catalysis, which is replaced by glutamine. CaclXIP was expressed as a recombinant protein in Pichia pastoris. Enzymatic assay showed that purified recombinant CaclXIP had only residual chitinolytic activity. However, it inhibited xylanases from Acrophialophora nainiana by approx. 60% when present at 12:1 (w/w) enzyme:inhibitor ratio. Additionally, CaclXIP at 1.5 ?g/?L inhibited the germination of spores of Phakopsora pachyrhizi by 45%. Conclusions: Our data suggests that CaclXIP belongs to a class of naturally inactive chitinases that have evolved to act in plant cell defence as xylanase inhibitors. Its role on inhibiting germination of fungal spores makes it an eligible candidate gene for the control of Asian rust.
650 $aPlant diseases and disorders
650 $aSoybeans
650 $aDoença de planta
650 $aSoja
700 1 $aSANTANA, C. G.
700 1 $aGODOY, C. V.
700 1 $aSEIXAS, C. D. S.
700 1 $aSILVA, M. S.
700 1 $aMOREIRA, L. R. S.
700 1 $aOLIVEIRA-NETO, O. B.
700 1 $aPRICE, D.
700 1 $aFITCHES, E.
700 1 $aFERREIRA FILHO, E. X.
700 1 $aMEHTA, A.
700 1 $aGATEHOUSE, J. A.
700 1 $aGROSSI-DE-SA, M. F.
773 $tBMC Biotechnology$gv. 11, 2011.
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Embrapa Recursos Genéticos e Biotecnologia (CENARGEN) |
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