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Registro Completo |
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Biblioteca(s): |
Embrapa Recursos Genéticos e Biotecnologia. |
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Data corrente: |
20/01/2015 |
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Data da última atualização: |
27/11/2023 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
BEZERRA, C. A.; MACEDO, L. L. P.; AMORIM, T. M. L.; SANTOS, V. O.; FRAGOSO, R. da R.; LUCENA, W. A.; MENEGUIM, A. M.; VALENCIA-JIMENEZ, A.; ENGLER, G.; SILVA, M. C. M.; ALBUQUERQUE, E. V. S.; GROSSI-DE-SA, M. F. |
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Afiliação: |
FURGS; FURGS; RODRIGO DA ROCHA FRAGOSO, CPAC; WAGNER ALEXANDRE LUCENA, CNPA; IAPAR; UNIVERSITY OF CALDAS, COLOMBIA; INSTITUT NATIONAL DE LA RECHERCHE AGRONOMIQUE, FRANCE; MARIA CRISTINA MATTAR DA SILVA, CENARGEN; ERIKA VALERIA SALIBA ALBUQUERQUE FR, CENARGEN; MARIA FATIMA GROSSI DE SA, CENARGEN. |
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Título: |
Molecular cloning and characterization of an α-amylase cDNA highly expressed in major feeding stages of the coffee berry borer, Hypothenemus hampei. |
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Ano de publicação: |
2014 |
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Fonte/Imprenta: |
Gene, v. 553, n. 1, p. 7-16, Dec. 2014. |
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DOI: |
10.1016/j.gene.2014.09.050 |
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Idioma: |
Inglês |
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Conteúdo: |
Abstract: a-Amylases are common enzymes responsible for hydrolyzing starch. Insect-pests, whose larvae develop in seeds, rely obligatorily on a-amylase activity to digest starch, as their major food source. Considering the relevance of insect a-amylases and the natural a-amylase inhibitors present in seeds to protect from insect damage, we report here the molecular cloning and nucleotide sequence of the full-length AmyHha cDNA of the coffee berry borer, Hypothenemus hampei, a major insect-pest of coffee crops. The AmyHha sequence has 1879 bp, containing a 1458 bp open reading frame, which encodes a predicted protein with 485 amino acid residues, with a predicted molecular mass of 51.2 kDa. The deduced protein showed 55?79% identity to other insect a-amylases, including Anthonomus grandis, Ips typographus and Sitophilus oryzae a-amylases. In depth analysis revealed that the highly conserved three amino acid residues (Asp184, Glu220, and Asp285), which compose the catalytic site are also presented in AmyHha amylase. The AmyHha gene seems to be a single copy in the haploid genome and AmyHha transcription levels were found higher in L2 larvae and adult insects, both corresponding to major feeding phases. Modeling of the AmyHha predicted protein uncovered striking structural similarities to the Tenebrio molitor a-amylase also displaying the same amino acid residues involved in enzyme catalysis (Asp184, Glu220 and Asp285). Since AmyHha gene was mostly transcribed in the intestinal tract of H. hampei larvae, the cognate a-amylase could be considered a high valuable target to coffee bean insect control by biotechnological strategies. MenosAbstract: a-Amylases are common enzymes responsible for hydrolyzing starch. Insect-pests, whose larvae develop in seeds, rely obligatorily on a-amylase activity to digest starch, as their major food source. Considering the relevance of insect a-amylases and the natural a-amylase inhibitors present in seeds to protect from insect damage, we report here the molecular cloning and nucleotide sequence of the full-length AmyHha cDNA of the coffee berry borer, Hypothenemus hampei, a major insect-pest of coffee crops. The AmyHha sequence has 1879 bp, containing a 1458 bp open reading frame, which encodes a predicted protein with 485 amino acid residues, with a predicted molecular mass of 51.2 kDa. The deduced protein showed 55?79% identity to other insect a-amylases, including Anthonomus grandis, Ips typographus and Sitophilus oryzae a-amylases. In depth analysis revealed that the highly conserved three amino acid residues (Asp184, Glu220, and Asp285), which compose the catalytic site are also presented in AmyHha amylase. The AmyHha gene seems to be a single copy in the haploid genome and AmyHha transcription levels were found higher in L2 larvae and adult insects, both corresponding to major feeding phases. Modeling of the AmyHha predicted protein uncovered striking structural similarities to the Tenebrio molitor a-amylase also displaying the same amino acid residues involved in enzyme catalysis (Asp184, Glu220 and Asp285). Since AmyHha gene was mostly transcribed in the intestinal... Mostrar Tudo |
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Palavras-Chave: |
Expressão gênica. |
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Thesagro: |
Amido; Curculionideo; Hidrolise; Praga de planta. |
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Thesaurus Nal: |
Curculionidae; Enzymatic hydrolysis; Gene expression; Insect pests; Starch. |
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Categoria do assunto: |
O Insetos e Entomologia |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/115999/1/34279.pdf
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Marc: |
LEADER 02795naa a2200385 a 4500
001 2006141
005 2023-11-27
008 2014 bl uuuu u00u1 u #d
024 7 $a10.1016/j.gene.2014.09.050$2DOI
100 1 $aBEZERRA, C. A.
245 $aMolecular cloning and characterization of an α-amylase cDNA highly expressed in major feeding stages of the coffee berry borer, Hypothenemus hampei.$h[electronic resource]
260 $c2014
520 $aAbstract: a-Amylases are common enzymes responsible for hydrolyzing starch. Insect-pests, whose larvae develop in seeds, rely obligatorily on a-amylase activity to digest starch, as their major food source. Considering the relevance of insect a-amylases and the natural a-amylase inhibitors present in seeds to protect from insect damage, we report here the molecular cloning and nucleotide sequence of the full-length AmyHha cDNA of the coffee berry borer, Hypothenemus hampei, a major insect-pest of coffee crops. The AmyHha sequence has 1879 bp, containing a 1458 bp open reading frame, which encodes a predicted protein with 485 amino acid residues, with a predicted molecular mass of 51.2 kDa. The deduced protein showed 55?79% identity to other insect a-amylases, including Anthonomus grandis, Ips typographus and Sitophilus oryzae a-amylases. In depth analysis revealed that the highly conserved three amino acid residues (Asp184, Glu220, and Asp285), which compose the catalytic site are also presented in AmyHha amylase. The AmyHha gene seems to be a single copy in the haploid genome and AmyHha transcription levels were found higher in L2 larvae and adult insects, both corresponding to major feeding phases. Modeling of the AmyHha predicted protein uncovered striking structural similarities to the Tenebrio molitor a-amylase also displaying the same amino acid residues involved in enzyme catalysis (Asp184, Glu220 and Asp285). Since AmyHha gene was mostly transcribed in the intestinal tract of H. hampei larvae, the cognate a-amylase could be considered a high valuable target to coffee bean insect control by biotechnological strategies.
650 $aCurculionidae
650 $aEnzymatic hydrolysis
650 $aGene expression
650 $aInsect pests
650 $aStarch
650 $aAmido
650 $aCurculionideo
650 $aHidrolise
650 $aPraga de planta
653 $aExpressão gênica
700 1 $aMACEDO, L. L. P.
700 1 $aAMORIM, T. M. L.
700 1 $aSANTOS, V. O.
700 1 $aFRAGOSO, R. da R.
700 1 $aLUCENA, W. A.
700 1 $aMENEGUIM, A. M.
700 1 $aVALENCIA-JIMENEZ, A.
700 1 $aENGLER, G.
700 1 $aSILVA, M. C. M.
700 1 $aALBUQUERQUE, E. V. S.
700 1 $aGROSSI-DE-SA, M. F.
773 $tGene$gv. 553, n. 1, p. 7-16, Dec. 2014.
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Registro original: |
Embrapa Recursos Genéticos e Biotecnologia (CENARGEN) |
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Registro Completo
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Biblioteca(s): |
Embrapa Florestas. |
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Data corrente: |
22/09/2020 |
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Data da última atualização: |
26/11/2020 |
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Autoria: |
DUARTE, D. M.; ROCHA, G. T.; RESENDE, C. L. P.; SILVA, B. M.; RODRIGUES, F. |
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Afiliação: |
UNIVERSIDADE FEDERAL DE UBERLÂNDIA; UNIVERSIDADE FEDERAL DE UBERLÂNDIA; UNIVERSIDADE ESTADUAL DE GOIÁS; UNIVERSIDADE ESTADUAL DE GOIÁS; UNIVERSIDADE ESTADUAL DE GOIÁS. |
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Título: |
Response of Schizolobium parahyba seedlings to water stress. |
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Ano de publicação: |
2020 |
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Fonte/Imprenta: |
Pesquisa Florestal Brasileira, Colombo, v. 40, e201801644, 2020. 5 p. |
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DOI: |
https://doi.org/10.4336/2020.pfb.40e201801644 |
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Idioma: |
Inglês |
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Notas: |
Nota científica. |
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Conteúdo: |
O objetivo deste trabalho foi identificar mecanismos de resposta ao estresse hídrico em mudas de Schizolobium parahyba Vell. Blake. Aos 90 dias após a emergência, as plantas foram submetidas a 10 dias de déficit hídrico, sendo irrigadas com diferentes porcentagens de evapotranspiração (20, 40, 60, 80 e 100%), por mais dez dias. No estágio inicial de desenvolvimento, as mudas de Schizolobium parahyba apresentaram tolerância parcial ao déficit hídrico causado e apresentaram um atraso na desidratação. Como estratégia de defesa, as plantas reduziram seu crescimento em altura, diâmetro e número de folhas, direcionando a produção de fotoassimilados para sua manutenção, com baixa taxa de transpiração. |
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Palavras-Chave: |
Estresse hídrico; Water deficiency. |
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Thesagro: |
Deficiência Hídrica; Evapotranspiração; Guapuruvu; Madeira; Schizolobium Parahyba. |
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Thesaurus NAL: |
Evapotranspiration. |
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Categoria do assunto: |
K Ciência Florestal e Produtos de Origem Vegetal |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/216137/1/1644-20565-1-PB.pdf
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Marc: |
LEADER 01588naa a2200289 a 4500
001 2125049
005 2020-11-26
008 2020 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.4336/2020.pfb.40e201801644$2DOI
100 1 $aDUARTE, D. M.
245 $aResponse of Schizolobium parahyba seedlings to water stress.$h[electronic resource]
260 $c2020
500 $aNota científica.
520 $aO objetivo deste trabalho foi identificar mecanismos de resposta ao estresse hídrico em mudas de Schizolobium parahyba Vell. Blake. Aos 90 dias após a emergência, as plantas foram submetidas a 10 dias de déficit hídrico, sendo irrigadas com diferentes porcentagens de evapotranspiração (20, 40, 60, 80 e 100%), por mais dez dias. No estágio inicial de desenvolvimento, as mudas de Schizolobium parahyba apresentaram tolerância parcial ao déficit hídrico causado e apresentaram um atraso na desidratação. Como estratégia de defesa, as plantas reduziram seu crescimento em altura, diâmetro e número de folhas, direcionando a produção de fotoassimilados para sua manutenção, com baixa taxa de transpiração.
650 $aEvapotranspiration
650 $aDeficiência Hídrica
650 $aEvapotranspiração
650 $aGuapuruvu
650 $aMadeira
650 $aSchizolobium Parahyba
653 $aEstresse hídrico
653 $aWater deficiency
700 1 $aROCHA, G. T.
700 1 $aRESENDE, C. L. P.
700 1 $aSILVA, B. M.
700 1 $aRODRIGUES, F.
773 $tPesquisa Florestal Brasileira, Colombo$gv. 40, e201801644, 2020. 5 p.
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Registro original: |
Embrapa Florestas (CNPF) |
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