Caracterização bioquímica da aldeído desidrogenase GmTP55 da soja (Glycine max)
Ano de defesa: | 2007 |
---|---|
Autor(a) principal: | |
Orientador(a): | |
Banca de defesa: | , |
Tipo de documento: | Dissertação |
Tipo de acesso: | Acesso aberto |
Idioma: | por |
Instituição de defesa: |
Universidade Federal de Viçosa
|
Programa de Pós-Graduação: |
Mestrado em Bioquímica Agrícola
|
Departamento: |
Bioquímica e Biologia molecular de plantas; Bioquímica e Biologia molecular animal
|
País: |
BR
|
Palavras-chave em Português: | |
Palavras-chave em Inglês: | |
Área do conhecimento CNPq: | |
Link de acesso: | http://locus.ufv.br/handle/123456789/2477 |
Resumo: | The protein GmTP55 (Glycine max turgor proten) belongs to the ALDH7 family, that falls into the superfamily of the aldehyde dehydrogenases (ALDH). Proteins of this family are structurally conserved and they have been identified by their accumulation in plants under abiotic stress conditions. Although they have been identified in several organisms, the physiological and biochemical function of proteins of the ALDH7 family have not been elucidated yet. In addition to sharing a high conservation of primary structure with other members of ALDH family, GmTP55 possesses several conserved domains and conserved amino acid at common positions of aldehyde dehydrogenases. To identify the biochemical function of the protein GmTP55, we expressed the protein in a prokaryotic expression system, and the enzymatic activity of the recombinant protein was tested using several aldehydes, as potential substrates. The protein GmTP55 exhibited a larger specificity for short-chain aliphatic aldehydes, as propionaldehyde, acetaldehyde, γ-aminobutiraldehyde and formaldehyde, oxidizing the carboxylic acids, in the presence of NAD+. Among the oxidized aldehydes, γ-aminobutiraldeido and formaldehyde may be considered as potential physiological substrates for GmTP55, as these aldehydes are produced as a result of the lipid peroxidation that occurs during the imposition of salt stress. The analysis of the physiological function of the protein GmTP55 was accomplished by using Arabidopsis thaliana plants ectopically expressing GmTP55 gene. Under conditions of salt stress, the seeds of transgenic plants exhibited a greater germination efficiency than the untransformed plants. Taken together, these results suggest that the protein GmTP55 is involved in plant tolerance to abiotic stresses and it acts in detoxification pathways of reactive aldehydes derived from lipid peroxidation. |
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Soares, Ana Paula Gomeshttp://lattes.cnpq.br/3631825469916595Fietto, Luciano Gomeshttp://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4763824H8Pereira, Maria Cristina Baracathttp://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4780021E6Fontes, Elizabeth Pacheco Batistahttp://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4781848H2Fietto, Juliana Lopes Rangelhttp://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4790238D0Moraes, George Henrique Kling dehttp://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4721569T72015-03-26T13:07:39Z2007-07-242015-03-26T13:07:39Z2007-03-21SOARES, Ana Paula Gomes. Biochemical characterization of the soybean (Glycine max) aldehyde dehydrogenase GmTP55. 2007. 86 f. Dissertação (Mestrado em Bioquímica e Biologia molecular de plantas; Bioquímica e Biologia molecular animal) - Universidade Federal de Viçosa, Viçosa, 2007.http://locus.ufv.br/handle/123456789/2477The protein GmTP55 (Glycine max turgor proten) belongs to the ALDH7 family, that falls into the superfamily of the aldehyde dehydrogenases (ALDH). Proteins of this family are structurally conserved and they have been identified by their accumulation in plants under abiotic stress conditions. Although they have been identified in several organisms, the physiological and biochemical function of proteins of the ALDH7 family have not been elucidated yet. In addition to sharing a high conservation of primary structure with other members of ALDH family, GmTP55 possesses several conserved domains and conserved amino acid at common positions of aldehyde dehydrogenases. To identify the biochemical function of the protein GmTP55, we expressed the protein in a prokaryotic expression system, and the enzymatic activity of the recombinant protein was tested using several aldehydes, as potential substrates. The protein GmTP55 exhibited a larger specificity for short-chain aliphatic aldehydes, as propionaldehyde, acetaldehyde, γ-aminobutiraldehyde and formaldehyde, oxidizing the carboxylic acids, in the presence of NAD+. Among the oxidized aldehydes, γ-aminobutiraldeido and formaldehyde may be considered as potential physiological substrates for GmTP55, as these aldehydes are produced as a result of the lipid peroxidation that occurs during the imposition of salt stress. The analysis of the physiological function of the protein GmTP55 was accomplished by using Arabidopsis thaliana plants ectopically expressing GmTP55 gene. Under conditions of salt stress, the seeds of transgenic plants exhibited a greater germination efficiency than the untransformed plants. Taken together, these results suggest that the protein GmTP55 is involved in plant tolerance to abiotic stresses and it acts in detoxification pathways of reactive aldehydes derived from lipid peroxidation.A proteína GmTP55 (Glycine max turgor protein) pertence à família ALDH7, das superfamílias das aldeído desidrogenases (ALDH). As proteínas desta família apresentam estrutura primária conservada e têm sido identificadas por se acumularem em plantas submetidas a condições de estresse abiótico. Embora elas tenham sido identificadas em diversos organismos, às funções fisiológica e bioquímica das proteínas da família ALDH7 ainda não foi elucidada. Além de compartilhar uma alta conservação de estrutura primária com outros membros da família ALDH, GmTP55 possui diversos domínios e aminoácidos conservados em posições, característicos de enzimas aldeído desidrogenases. A fim de confirmar sua atividade enzimática, a proteína GmTP55 foi expressa em sistema heterólogo procarioto de expressão e a atividade da proteína recombinante foi testada usando diversos aldeídos como substratos em potencial. A proteína GmTP55 apresentou maior atividade sobre aldeídos alifáticos de cadeia curta como propionaldeído, acetaldeído, γ-aminobutiraldeído e formaldeído, oxidando-os a ácidos carboxílicos na presença de NAD+. Dentre os aldeídos oxidados, o γ-aminobutiraldeido e formaldeído podem ser considerados como substratos fisiológicos potenciais para GmTP55, visto que estes aldeídos são produzidos como resultado da peroxidação de lipídios que ocorre durante a imposição de estresse celular oxidativo. A análise da função fisiológica da proteína GmTP55 foi realizada com plantas de Arabidopsis thaliana expressando ectopicamente o gene GmTP55. As plantas transgênicas obtidas, expressando constitutivamente a proteína, tiveram suas sementes plaqueadas em condições de estresse salino. Nestas condições, as plantas transgênicas apresentaram maior eficiência de germinação do que as plantas não transformadas. Coletivamente, estes resultados sugerem que a proteína GmTP55 está envolvida na tolerância das plantas a estresses abióticos, atuando em vias de detoxificação celular de aldeídos reativos derivados de peroxidação de lipídios.Universidade Estadual do Sudoeste da Bahiaapplication/pdfporUniversidade Federal de ViçosaMestrado em Bioquímica AgrícolaUFVBRBioquímica e Biologia molecular de plantas; Bioquímica e Biologia molecular animalAldeído desidrogenaseGlycine maxSojaAldehyde dehydrogenaseGlycine maxSoybeanCNPQ::CIENCIAS BIOLOGICAS::BIOQUIMICA::BIOLOGIA MOLECULARCaracterização bioquímica da aldeído desidrogenase GmTP55 da soja (Glycine max)Biochemical characterization of the soybean (Glycine max) aldehyde dehydrogenase GmTP55info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisinfo:eu-repo/semantics/openAccessreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFVORIGINALtexto completo.pdfapplication/pdf1322059https://locus.ufv.br//bitstream/123456789/2477/1/texto%20completo.pdff57b393d31fdd28ecc81b7d2ede08c38MD51TEXTtexto completo.pdf.txttexto completo.pdf.txtExtracted texttext/plain160751https://locus.ufv.br//bitstream/123456789/2477/2/texto%20completo.pdf.txt62dda1bf554709bcad33d6a2662420c2MD52THUMBNAILtexto completo.pdf.jpgtexto completo.pdf.jpgIM Thumbnailimage/jpeg3528https://locus.ufv.br//bitstream/123456789/2477/3/texto%20completo.pdf.jpgd9eeb42436ac4d03b132d4cb5628f728MD53123456789/24772016-04-08 23:06:11.184oai:locus.ufv.br:123456789/2477Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452016-04-09T02:06:11LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false |
dc.title.por.fl_str_mv |
Caracterização bioquímica da aldeído desidrogenase GmTP55 da soja (Glycine max) |
dc.title.alternative.eng.fl_str_mv |
Biochemical characterization of the soybean (Glycine max) aldehyde dehydrogenase GmTP55 |
title |
Caracterização bioquímica da aldeído desidrogenase GmTP55 da soja (Glycine max) |
spellingShingle |
Caracterização bioquímica da aldeído desidrogenase GmTP55 da soja (Glycine max) Soares, Ana Paula Gomes Aldeído desidrogenase Glycine max Soja Aldehyde dehydrogenase Glycine max Soybean CNPQ::CIENCIAS BIOLOGICAS::BIOQUIMICA::BIOLOGIA MOLECULAR |
title_short |
Caracterização bioquímica da aldeído desidrogenase GmTP55 da soja (Glycine max) |
title_full |
Caracterização bioquímica da aldeído desidrogenase GmTP55 da soja (Glycine max) |
title_fullStr |
Caracterização bioquímica da aldeído desidrogenase GmTP55 da soja (Glycine max) |
title_full_unstemmed |
Caracterização bioquímica da aldeído desidrogenase GmTP55 da soja (Glycine max) |
title_sort |
Caracterização bioquímica da aldeído desidrogenase GmTP55 da soja (Glycine max) |
author |
Soares, Ana Paula Gomes |
author_facet |
Soares, Ana Paula Gomes |
author_role |
author |
dc.contributor.authorLattes.por.fl_str_mv |
http://lattes.cnpq.br/3631825469916595 |
dc.contributor.author.fl_str_mv |
Soares, Ana Paula Gomes |
dc.contributor.advisor-co1.fl_str_mv |
Fietto, Luciano Gomes |
dc.contributor.advisor-co1Lattes.fl_str_mv |
http://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4763824H8 |
dc.contributor.advisor-co2.fl_str_mv |
Pereira, Maria Cristina Baracat |
dc.contributor.advisor-co2Lattes.fl_str_mv |
http://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4780021E6 |
dc.contributor.advisor1.fl_str_mv |
Fontes, Elizabeth Pacheco Batista |
dc.contributor.advisor1Lattes.fl_str_mv |
http://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4781848H2 |
dc.contributor.referee1.fl_str_mv |
Fietto, Juliana Lopes Rangel |
dc.contributor.referee1Lattes.fl_str_mv |
http://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4790238D0 |
dc.contributor.referee2.fl_str_mv |
Moraes, George Henrique Kling de |
dc.contributor.referee2Lattes.fl_str_mv |
http://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4721569T7 |
contributor_str_mv |
Fietto, Luciano Gomes Pereira, Maria Cristina Baracat Fontes, Elizabeth Pacheco Batista Fietto, Juliana Lopes Rangel Moraes, George Henrique Kling de |
dc.subject.por.fl_str_mv |
Aldeído desidrogenase Glycine max Soja |
topic |
Aldeído desidrogenase Glycine max Soja Aldehyde dehydrogenase Glycine max Soybean CNPQ::CIENCIAS BIOLOGICAS::BIOQUIMICA::BIOLOGIA MOLECULAR |
dc.subject.eng.fl_str_mv |
Aldehyde dehydrogenase Glycine max Soybean |
dc.subject.cnpq.fl_str_mv |
CNPQ::CIENCIAS BIOLOGICAS::BIOQUIMICA::BIOLOGIA MOLECULAR |
description |
The protein GmTP55 (Glycine max turgor proten) belongs to the ALDH7 family, that falls into the superfamily of the aldehyde dehydrogenases (ALDH). Proteins of this family are structurally conserved and they have been identified by their accumulation in plants under abiotic stress conditions. Although they have been identified in several organisms, the physiological and biochemical function of proteins of the ALDH7 family have not been elucidated yet. In addition to sharing a high conservation of primary structure with other members of ALDH family, GmTP55 possesses several conserved domains and conserved amino acid at common positions of aldehyde dehydrogenases. To identify the biochemical function of the protein GmTP55, we expressed the protein in a prokaryotic expression system, and the enzymatic activity of the recombinant protein was tested using several aldehydes, as potential substrates. The protein GmTP55 exhibited a larger specificity for short-chain aliphatic aldehydes, as propionaldehyde, acetaldehyde, γ-aminobutiraldehyde and formaldehyde, oxidizing the carboxylic acids, in the presence of NAD+. Among the oxidized aldehydes, γ-aminobutiraldeido and formaldehyde may be considered as potential physiological substrates for GmTP55, as these aldehydes are produced as a result of the lipid peroxidation that occurs during the imposition of salt stress. The analysis of the physiological function of the protein GmTP55 was accomplished by using Arabidopsis thaliana plants ectopically expressing GmTP55 gene. Under conditions of salt stress, the seeds of transgenic plants exhibited a greater germination efficiency than the untransformed plants. Taken together, these results suggest that the protein GmTP55 is involved in plant tolerance to abiotic stresses and it acts in detoxification pathways of reactive aldehydes derived from lipid peroxidation. |
publishDate |
2007 |
dc.date.available.fl_str_mv |
2007-07-24 2015-03-26T13:07:39Z |
dc.date.issued.fl_str_mv |
2007-03-21 |
dc.date.accessioned.fl_str_mv |
2015-03-26T13:07:39Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/masterThesis |
format |
masterThesis |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
SOARES, Ana Paula Gomes. Biochemical characterization of the soybean (Glycine max) aldehyde dehydrogenase GmTP55. 2007. 86 f. Dissertação (Mestrado em Bioquímica e Biologia molecular de plantas; Bioquímica e Biologia molecular animal) - Universidade Federal de Viçosa, Viçosa, 2007. |
dc.identifier.uri.fl_str_mv |
http://locus.ufv.br/handle/123456789/2477 |
identifier_str_mv |
SOARES, Ana Paula Gomes. Biochemical characterization of the soybean (Glycine max) aldehyde dehydrogenase GmTP55. 2007. 86 f. Dissertação (Mestrado em Bioquímica e Biologia molecular de plantas; Bioquímica e Biologia molecular animal) - Universidade Federal de Viçosa, Viçosa, 2007. |
url |
http://locus.ufv.br/handle/123456789/2477 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
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application/pdf |
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Universidade Federal de Viçosa |
dc.publisher.program.fl_str_mv |
Mestrado em Bioquímica Agrícola |
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UFV |
dc.publisher.country.fl_str_mv |
BR |
dc.publisher.department.fl_str_mv |
Bioquímica e Biologia molecular de plantas; Bioquímica e Biologia molecular animal |
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Universidade Federal de Viçosa |
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reponame:LOCUS Repositório Institucional da UFV instname:Universidade Federal de Viçosa (UFV) instacron:UFV |
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