Cloning Expression and Characterization of Methionine Adenosyltransferase in Leishmania infantumPromastigotes

[EN] Methionine adenosyltransferase (MAT) catalyzes the synthesis of s-adenosylmethionine (AdoMet), a metabolite that plays an important role in a variety of cellular functions, such as methylation, sulfuration, and polyamine synthesis. In this study, genomic DNA from the protozoan parasite Leishman...

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Autores: Reguera Torres, Rosa María, Balaña Fouce, Rafael, Pérez Pertejo, Maria Yolanda, Fernández, Francisco J., García Estrada, Carlos, Cubría García, Juan Carlos, Ordóñez Pascua, César, Ordóñez, David
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2002
País:España
Institución:Universidad de León
Repositorio:BULERIA. Repositorio Institucional de la Universidad de León
OAI Identifier:oai:buleria.unileon.es:10612/24316
Acceso en línea:https://www.sciencedirect.com/science/article/pii/S0021925820875954?via%3Dihub
https://hdl.handle.net/10612/24316
Access Level:acceso abierto
Palabra clave:Toxicología
Methionine Adenosyltransferase
Leishmania infantum
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spelling Cloning Expression and Characterization of Methionine Adenosyltransferase in Leishmania infantumPromastigotesReguera Torres, Rosa MaríaBalaña Fouce, RafaelPérez Pertejo, Maria YolandaFernández, Francisco J.García Estrada, CarlosCubría García, Juan CarlosOrdóñez Pascua, CésarOrdóñez, DavidToxicologíaMethionine AdenosyltransferaseLeishmania infantum[EN] Methionine adenosyltransferase (MAT) catalyzes the synthesis of s-adenosylmethionine (AdoMet), a metabolite that plays an important role in a variety of cellular functions, such as methylation, sulfuration, and polyamine synthesis. In this study, genomic DNA from the protozoan parasite Leishmania infantum was cloned and characterized. L. infantum MAT, unlike mammalian MAT, is codified by two identical genes in a tandem arrangement and is only weakly regulated by AdoMet. L. infantum MAT mRNA is expressed as a single transcript, with the enzyme forming a homodimer with tripolyphosphatase in addition to MAT activity. Expression of L. infantum MAT in Escherichia coli proves that the MAT and tripolyphosphatase activities are functional in vivo. MAT shows sigmoidal behavior and is weakly inhibited by AdoMet, whereas tripolyphosphatase activity has sigmoidal behavior and is strongly activated by AdoMet. Plasmids containing the regions flanking MAT2 were fused immediately upstream and downstream of the luciferase-coding region and transfected into L. infantum. Subsequent examination of luciferase activity showed that homologous expression in L. infantum promastigotes was dramatically dependent on the presence of polypyrimidine tracts and a spliced leader junction site upstream of the luciferase gene, whereas downstream sequences appeared to have no bearing on expression.SIElsevierToxicologiaFacultad de Veterinaria2002info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttps://www.sciencedirect.com/science/article/pii/S0021925820875954?via%3Dihubhttps://hdl.handle.net/10612/24316reponame:BULERIA. Repositorio Institucional de la Universidad de Leóninstname:Universidad de LeónIngléshttp://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessoai:buleria.unileon.es:10612/243162026-06-24T12:43:27Z
dc.title.none.fl_str_mv Cloning Expression and Characterization of Methionine Adenosyltransferase in Leishmania infantumPromastigotes
title Cloning Expression and Characterization of Methionine Adenosyltransferase in Leishmania infantumPromastigotes
spellingShingle Cloning Expression and Characterization of Methionine Adenosyltransferase in Leishmania infantumPromastigotes
Reguera Torres, Rosa María
Toxicología
Methionine Adenosyltransferase
Leishmania infantum
title_short Cloning Expression and Characterization of Methionine Adenosyltransferase in Leishmania infantumPromastigotes
title_full Cloning Expression and Characterization of Methionine Adenosyltransferase in Leishmania infantumPromastigotes
title_fullStr Cloning Expression and Characterization of Methionine Adenosyltransferase in Leishmania infantumPromastigotes
title_full_unstemmed Cloning Expression and Characterization of Methionine Adenosyltransferase in Leishmania infantumPromastigotes
title_sort Cloning Expression and Characterization of Methionine Adenosyltransferase in Leishmania infantumPromastigotes
dc.creator.none.fl_str_mv Reguera Torres, Rosa María
Balaña Fouce, Rafael
Pérez Pertejo, Maria Yolanda
Fernández, Francisco J.
García Estrada, Carlos
Cubría García, Juan Carlos
Ordóñez Pascua, César
Ordóñez, David
author Reguera Torres, Rosa María
author_facet Reguera Torres, Rosa María
Balaña Fouce, Rafael
Pérez Pertejo, Maria Yolanda
Fernández, Francisco J.
García Estrada, Carlos
Cubría García, Juan Carlos
Ordóñez Pascua, César
Ordóñez, David
author_role author
author2 Balaña Fouce, Rafael
Pérez Pertejo, Maria Yolanda
Fernández, Francisco J.
García Estrada, Carlos
Cubría García, Juan Carlos
Ordóñez Pascua, César
Ordóñez, David
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Toxicologia
Facultad de Veterinaria
dc.subject.none.fl_str_mv Toxicología
Methionine Adenosyltransferase
Leishmania infantum
topic Toxicología
Methionine Adenosyltransferase
Leishmania infantum
description [EN] Methionine adenosyltransferase (MAT) catalyzes the synthesis of s-adenosylmethionine (AdoMet), a metabolite that plays an important role in a variety of cellular functions, such as methylation, sulfuration, and polyamine synthesis. In this study, genomic DNA from the protozoan parasite Leishmania infantum was cloned and characterized. L. infantum MAT, unlike mammalian MAT, is codified by two identical genes in a tandem arrangement and is only weakly regulated by AdoMet. L. infantum MAT mRNA is expressed as a single transcript, with the enzyme forming a homodimer with tripolyphosphatase in addition to MAT activity. Expression of L. infantum MAT in Escherichia coli proves that the MAT and tripolyphosphatase activities are functional in vivo. MAT shows sigmoidal behavior and is weakly inhibited by AdoMet, whereas tripolyphosphatase activity has sigmoidal behavior and is strongly activated by AdoMet. Plasmids containing the regions flanking MAT2 were fused immediately upstream and downstream of the luciferase-coding region and transfected into L. infantum. Subsequent examination of luciferase activity showed that homologous expression in L. infantum promastigotes was dramatically dependent on the presence of polypyrimidine tracts and a spliced leader junction site upstream of the luciferase gene, whereas downstream sequences appeared to have no bearing on expression.
publishDate 2002
dc.date.none.fl_str_mv 2002
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://www.sciencedirect.com/science/article/pii/S0021925820875954?via%3Dihub
https://hdl.handle.net/10612/24316
url https://www.sciencedirect.com/science/article/pii/S0021925820875954?via%3Dihub
https://hdl.handle.net/10612/24316
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.rights.none.fl_str_mv http://creativecommons.org/licenses/by-nc-nd/4.0/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:BULERIA. Repositorio Institucional de la Universidad de León
instname:Universidad de León
instname_str Universidad de León
reponame_str BULERIA. Repositorio Institucional de la Universidad de León
collection BULERIA. Repositorio Institucional de la Universidad de León
repository.name.fl_str_mv
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