Please use this identifier to cite or link to this item: http://www.alice.cnptia.embrapa.br/alice/handle/doc/1006141
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dc.contributor.authorBEZERRA, C. A.
dc.contributor.authorMACEDO, L. L. P.
dc.contributor.authorAMORIM, T. M. L.
dc.contributor.authorSANTOS, V. O.
dc.contributor.authorFRAGOSO, R. da R.
dc.contributor.authorLUCENA, W. A.
dc.contributor.authorMENEGUIM, A. M.
dc.contributor.authorVALENCIA-JIMENEZ, A.
dc.contributor.authorENGLER, G.
dc.contributor.authorSILVA, M. C. M.
dc.contributor.authorALBUQUERQUE, E. V. S.
dc.contributor.authorGROSSI-DE-SA, M. F.
dc.contributor.otherFURGS; 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.
dc.date.accessioned2020-11-03T09:16:26Z-
dc.date.available2020-11-03T09:16:26Z-
dc.date.created2015-01-20
dc.date.issued2014
dc.identifier.other35746
dc.identifier.urihttp://www.alice.cnptia.embrapa.br/alice/handle/doc/1006141-
dc.descriptionAbstract: 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.
dc.description.uribitstream/item/115999/1/34279.pdf
dc.languageIngles
dc.language.isoen
dc.publisherGene, v. 553, n. 1, p. 7-16, Dec. 2014.
dc.relation.ispartofEmbrapa Recursos Genéticos e Biotecnologia - Artigo em periódico indexado (ALICE)
dc.subjectExpressão gênica
dc.titleMolecular cloning and characterization of an alfa-amylase cDNA highly expressed in major feeding stages of the coffee berry borer, Hypothenemus hampei.
dc.typeArtigo em periódico indexado (ALICE)
dc.subject.thesagroCurculionideo
dc.subject.thesagroPraga de planta
dc.subject.thesagroAmido
dc.subject.thesagroHidrolise
dc.subject.nalthesaurusCurculionidae
dc.subject.nalthesaurusGene expression
dc.subject.nalthesaurusInsect pests
dc.subject.nalthesaurusStarch
dc.subject.nalthesaurusEnzymatic hydrolysis
dc.ainfo.id1006141
dc.ainfo.lastupdate2018-07-11
dc.identifier.doi10.1016/j.gene.2014.09.050
Appears in Collections:Artigo em periódico indexado (CENARGEN)

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