Clonagem, expressão heteróloga e interações intermoleculares da proteína aspartato semialdeído desidrogenase de Paracoccidioides brasiliensis
Autor(a) principal: | |
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Data de Publicação: | 2017 |
Tipo de documento: | Dissertação |
Idioma: | por |
Título da fonte: | Repositório Institucional da UFG |
Texto Completo: | http://repositorio.bc.ufg.br/tede/handle/tede/9114 |
Resumo: | Paracoccidioides comprises the genus of fungi causing paracoccidioidomycosis. The research of new treatments, especially those based on inhibition of metabolic pathways important for microorganisms has gained prominence and the aspartate pathway, necessary for the biosynthesis of threonine, isoleucine and methionine in microorganisms, is not found in humans. Catalyzing the second step of this pathway, we found aspartate semialdehyde dehydrogenase (ASADH), which has not yet been characterized in Paracoccidioides spp. and has no substituents in its catalytic function in the aspartate pathway. Thus, it is of interest the determination of its biological properties experimentally that their biological properties be determined experimentally. ASADH from Pb18 was cloned into vector pGEX-4T3, expressed in E. coli Stellar cells and purified on a glutathione-sepharose column. Then, antibodies were produced and used in Western blot assay to confirm protein expression. The pull-down-GST assay was performed and allowed the identification of complexes of interactions between ASADH and soluble proteins present in total protein extract of the yeast form of Pb18. Interactions with proteins of several functional categories, among them those related to the metabolism of threonine, isoleucine and methionine, were found, reinforcing the performance of ASADH in the amino acid biosynthesis of Pb18, as well as proteins related to substrate supply to the aspartate pathway and proteins that use metabolites of this pathway. Interactions with proteins involved in other metabolic pathways were also observed, as well as unprecedented interactions, suggesting the importance of ASADH in the functional processes of microorganisms. |
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Pereira, Maristelahttp://lattes.cnpq.br/1345781867765758Pereira, MaristelaRocha, Juliana Alves ParenteBailão, Mirelle Garcia Silvahttp://lattes.cnpq.br/7976114156286508Nascimento, Thaylla Horbylon2018-12-03T13:14:23Z2017-12-12NASCIMENTO, T. H. Clonagem, expressão heteróloga e interações intermoleculares da proteína aspartato semialdeído desidrogenase de Paracoccidioides brasiliensis. 2017. 79 f. Dissertação (Mestrado em Genética e Biologia Molecular) - Universidade Federal de Goiás, Goiânia, 2017.http://repositorio.bc.ufg.br/tede/handle/tede/9114Paracoccidioides comprises the genus of fungi causing paracoccidioidomycosis. The research of new treatments, especially those based on inhibition of metabolic pathways important for microorganisms has gained prominence and the aspartate pathway, necessary for the biosynthesis of threonine, isoleucine and methionine in microorganisms, is not found in humans. Catalyzing the second step of this pathway, we found aspartate semialdehyde dehydrogenase (ASADH), which has not yet been characterized in Paracoccidioides spp. and has no substituents in its catalytic function in the aspartate pathway. Thus, it is of interest the determination of its biological properties experimentally that their biological properties be determined experimentally. ASADH from Pb18 was cloned into vector pGEX-4T3, expressed in E. coli Stellar cells and purified on a glutathione-sepharose column. Then, antibodies were produced and used in Western blot assay to confirm protein expression. The pull-down-GST assay was performed and allowed the identification of complexes of interactions between ASADH and soluble proteins present in total protein extract of the yeast form of Pb18. Interactions with proteins of several functional categories, among them those related to the metabolism of threonine, isoleucine and methionine, were found, reinforcing the performance of ASADH in the amino acid biosynthesis of Pb18, as well as proteins related to substrate supply to the aspartate pathway and proteins that use metabolites of this pathway. Interactions with proteins involved in other metabolic pathways were also observed, as well as unprecedented interactions, suggesting the importance of ASADH in the functional processes of microorganisms.Paracoccidioides compreende o gênero de fungos causadores da paracoccidioidomicose. A pesquisa de novos tratamentos, sobretudo aqueles baseados em inibição de vias metabólicas importantes para micro-organismos, tem ganhado destaque e a via do aspartato não é encontrada em humanos. A via do aspartato é necessária para a síntese de treonina, isoleucina e metionina. Catalisando o segundo passo dessa via, encontramos a aspartato semialdeído desidrogenase (ASADH), que ainda não foi caracterizada em Paracoccidioides spp. e não possui substituintes em sua função catalítica na via do aspartato. Assim, é de interesse que suas propriedades biológicas sejam determinadas experimentalmente. A ASADH proveniente de Pb18 foi clonada em vetor pGEX-4T3, expressa em células E. coli Stellar e purificada em coluna de glutationa-sefarose. Em seguida, anticorpos foram produzidos e utilizados em ensaio de Western-blot para confirmar a expressão proteica. O ensaio de pull-down-GST foi realizado e permitiu a identificação de complexos de interações entre a ASADH e proteínas solúveis presentes em extrato proteico total da forma de levedura de Pb18. Foram encontradas interações com proteínas de diversas categorias funcionais, dentre elas relacionadas ao metabolismo de treonina, isoleucina e metionina, reforçando a atuação da ASADH na biossíntese de aminoácidos de Pb18, bem como proteínas relacionadas ao fornecimento de substrato para a via do aspartato e proteínas que utilizam os metabólitos dessa via. Também foram observadas interações com proteínas envolvidas em outras vias metabólicas, assim como interações inéditas, sugerindo a importância de ASADH nos processos funcionais de micro-organismos.Submitted by Ana Caroline Costa (ana_caroline212@hotmail.com) on 2018-11-30T18:44:39Z No. of bitstreams: 2 Dissertação - Thaylla Horbylon Nascimento - 2017.pdf: 2748481 bytes, checksum: 12679d6d81f935cee0a82be36ee7480a (MD5) license_rdf: 0 bytes, checksum: d41d8cd98f00b204e9800998ecf8427e (MD5)Approved for entry into archive by Luciana Ferreira (lucgeral@gmail.com) on 2018-12-03T13:14:23Z (GMT) No. of bitstreams: 2 Dissertação - Thaylla Horbylon Nascimento - 2017.pdf: 2748481 bytes, checksum: 12679d6d81f935cee0a82be36ee7480a (MD5) license_rdf: 0 bytes, checksum: d41d8cd98f00b204e9800998ecf8427e (MD5)Made available in DSpace on 2018-12-03T13:14:23Z (GMT). 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dc.title.eng.fl_str_mv |
Clonagem, expressão heteróloga e interações intermoleculares da proteína aspartato semialdeído desidrogenase de Paracoccidioides brasiliensis |
dc.title.alternative.eng.fl_str_mv |
Cloning, heterologous expression and intermolecular interactions of the protein aspartate semialdehyde dehydrogenase from Paracoccidioides brasiliensis |
title |
Clonagem, expressão heteróloga e interações intermoleculares da proteína aspartato semialdeído desidrogenase de Paracoccidioides brasiliensis |
spellingShingle |
Clonagem, expressão heteróloga e interações intermoleculares da proteína aspartato semialdeído desidrogenase de Paracoccidioides brasiliensis Nascimento, Thaylla Horbylon ASADH Paracoccidioides brasiliensis Pull-down GST GENETICA::GENETICA MOLECULAR E DE MICROORGANISMOS |
title_short |
Clonagem, expressão heteróloga e interações intermoleculares da proteína aspartato semialdeído desidrogenase de Paracoccidioides brasiliensis |
title_full |
Clonagem, expressão heteróloga e interações intermoleculares da proteína aspartato semialdeído desidrogenase de Paracoccidioides brasiliensis |
title_fullStr |
Clonagem, expressão heteróloga e interações intermoleculares da proteína aspartato semialdeído desidrogenase de Paracoccidioides brasiliensis |
title_full_unstemmed |
Clonagem, expressão heteróloga e interações intermoleculares da proteína aspartato semialdeído desidrogenase de Paracoccidioides brasiliensis |
title_sort |
Clonagem, expressão heteróloga e interações intermoleculares da proteína aspartato semialdeído desidrogenase de Paracoccidioides brasiliensis |
author |
Nascimento, Thaylla Horbylon |
author_facet |
Nascimento, Thaylla Horbylon |
author_role |
author |
dc.contributor.advisor1.fl_str_mv |
Pereira, Maristela |
dc.contributor.advisor1Lattes.fl_str_mv |
http://lattes.cnpq.br/1345781867765758 |
dc.contributor.referee1.fl_str_mv |
Pereira, Maristela |
dc.contributor.referee2.fl_str_mv |
Rocha, Juliana Alves Parente |
dc.contributor.referee3.fl_str_mv |
Bailão, Mirelle Garcia Silva |
dc.contributor.authorLattes.fl_str_mv |
http://lattes.cnpq.br/7976114156286508 |
dc.contributor.author.fl_str_mv |
Nascimento, Thaylla Horbylon |
contributor_str_mv |
Pereira, Maristela Pereira, Maristela Rocha, Juliana Alves Parente Bailão, Mirelle Garcia Silva |
dc.subject.por.fl_str_mv |
ASADH Paracoccidioides brasiliensis |
topic |
ASADH Paracoccidioides brasiliensis Pull-down GST GENETICA::GENETICA MOLECULAR E DE MICROORGANISMOS |
dc.subject.eng.fl_str_mv |
Pull-down GST |
dc.subject.cnpq.fl_str_mv |
GENETICA::GENETICA MOLECULAR E DE MICROORGANISMOS |
description |
Paracoccidioides comprises the genus of fungi causing paracoccidioidomycosis. The research of new treatments, especially those based on inhibition of metabolic pathways important for microorganisms has gained prominence and the aspartate pathway, necessary for the biosynthesis of threonine, isoleucine and methionine in microorganisms, is not found in humans. Catalyzing the second step of this pathway, we found aspartate semialdehyde dehydrogenase (ASADH), which has not yet been characterized in Paracoccidioides spp. and has no substituents in its catalytic function in the aspartate pathway. Thus, it is of interest the determination of its biological properties experimentally that their biological properties be determined experimentally. ASADH from Pb18 was cloned into vector pGEX-4T3, expressed in E. coli Stellar cells and purified on a glutathione-sepharose column. Then, antibodies were produced and used in Western blot assay to confirm protein expression. The pull-down-GST assay was performed and allowed the identification of complexes of interactions between ASADH and soluble proteins present in total protein extract of the yeast form of Pb18. Interactions with proteins of several functional categories, among them those related to the metabolism of threonine, isoleucine and methionine, were found, reinforcing the performance of ASADH in the amino acid biosynthesis of Pb18, as well as proteins related to substrate supply to the aspartate pathway and proteins that use metabolites of this pathway. Interactions with proteins involved in other metabolic pathways were also observed, as well as unprecedented interactions, suggesting the importance of ASADH in the functional processes of microorganisms. |
publishDate |
2017 |
dc.date.issued.fl_str_mv |
2017-12-12 |
dc.date.accessioned.fl_str_mv |
2018-12-03T13:14:23Z |
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info:eu-repo/semantics/publishedVersion |
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info:eu-repo/semantics/masterThesis |
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dc.identifier.citation.fl_str_mv |
NASCIMENTO, T. H. Clonagem, expressão heteróloga e interações intermoleculares da proteína aspartato semialdeído desidrogenase de Paracoccidioides brasiliensis. 2017. 79 f. Dissertação (Mestrado em Genética e Biologia Molecular) - Universidade Federal de Goiás, Goiânia, 2017. |
dc.identifier.uri.fl_str_mv |
http://repositorio.bc.ufg.br/tede/handle/tede/9114 |
identifier_str_mv |
NASCIMENTO, T. H. Clonagem, expressão heteróloga e interações intermoleculares da proteína aspartato semialdeído desidrogenase de Paracoccidioides brasiliensis. 2017. 79 f. Dissertação (Mestrado em Genética e Biologia Molecular) - Universidade Federal de Goiás, Goiânia, 2017. |
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http://repositorio.bc.ufg.br/tede/handle/tede/9114 |
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por |
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http://creativecommons.org/licenses/by-nc-nd/4.0/ info:eu-repo/semantics/openAccess |
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http://creativecommons.org/licenses/by-nc-nd/4.0/ |
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Universidade Federal de Goiás |
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UFG |
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Universidade Federal de Goiás |
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