Occurrence, structure, and evolution of nitric oxide synthase-like proteins in the plant kingdom

Autores
Jeandroz, Sylvain; Wipf, Daniel; Stuehr, Dennis J.; Lamattina, Lorenzo; Melkonian, Michael; Tian, Zhijian; Zhu, Ying; Carpenter, Eric J.; Wong, Gane Ka-Shu; Wendehenne, David
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Nitric oxide (NO) signaling regulates various physiological processes in both animals and plants. In animals, NO synthesis is mainly catalyzed by NO synthase (NOS) enzymes. Although NOS-like activities that are sensitive to mammalian NOS inhibitors have been detected in plant extracts, few bona fide plant NOS enzymes have been identified. We searched the data set produced by the 1000 Plants (1KP) international consortium for the presence of transcripts encoding NOS-like proteins in over 1000 species of land plants and algae. We also searched for genes encoding NOS-like enzymes in 24 publicly available algal genomes. We identified no typical NOS sequences in 1087 sequenced transcriptomes of land plants. In contrast, we identified NOS-like sequences in 15 of the 265 algal species analyzed. Even if the presence of NOS enzymes assembled from multipolypeptides in plants cannot be conclusively discarded, the emerging data suggest that, instead of generating NO with evolutionarily conserved NOS enzymes, land plants have evolved finely regulated nitrate assimilation and reduction processes to synthesize NO through a mechanism different than that in animals.
Fil: Jeandroz, Sylvain. AgroSup Dijon; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Wipf, Daniel. Universite de Bourgogne; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Stuehr, Dennis J.. Lerner Research Institute; Estados Unidos
Fil: Lamattina, Lorenzo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: Melkonian, Michael. Universitat zu Köln; Alemania
Fil: Tian, Zhijian. BGI Shenzhen; China
Fil: Zhu, Ying. BGI Shenzhen; China
Fil: Carpenter, Eric J.. University of Alberta; Canadá
Fil: Wong, Gane Ka-Shu. University of Alberta; Canadá. BGI Shenzhen; China
Fil: Wendehenne, David. Centre National de la Recherche Scientifique; Francia. Universite de Bourgogne; Francia
Materia
Nitric Oxide
Nitric Oxide Synthase
Plantae
Evolution
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/56197
Acceder
id CONICETDig_d226972e615effcbd153cf1db206bbbc
oai_identifier_str oai:ri.conicet.gov.ar:11336/56197
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Occurrence, structure, and evolution of nitric oxide synthase-like proteins in the plant kingdomJeandroz, SylvainWipf, DanielStuehr, Dennis J.Lamattina, LorenzoMelkonian, MichaelTian, ZhijianZhu, YingCarpenter, Eric J.Wong, Gane Ka-ShuWendehenne, DavidNitric OxideNitric Oxide SynthasePlantaeEvolutionhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Nitric oxide (NO) signaling regulates various physiological processes in both animals and plants. In animals, NO synthesis is mainly catalyzed by NO synthase (NOS) enzymes. Although NOS-like activities that are sensitive to mammalian NOS inhibitors have been detected in plant extracts, few bona fide plant NOS enzymes have been identified. We searched the data set produced by the 1000 Plants (1KP) international consortium for the presence of transcripts encoding NOS-like proteins in over 1000 species of land plants and algae. We also searched for genes encoding NOS-like enzymes in 24 publicly available algal genomes. We identified no typical NOS sequences in 1087 sequenced transcriptomes of land plants. In contrast, we identified NOS-like sequences in 15 of the 265 algal species analyzed. Even if the presence of NOS enzymes assembled from multipolypeptides in plants cannot be conclusively discarded, the emerging data suggest that, instead of generating NO with evolutionarily conserved NOS enzymes, land plants have evolved finely regulated nitrate assimilation and reduction processes to synthesize NO through a mechanism different than that in animals.Fil: Jeandroz, Sylvain. AgroSup Dijon; Francia. Centre National de la Recherche Scientifique; FranciaFil: Wipf, Daniel. Universite de Bourgogne; Francia. Centre National de la Recherche Scientifique; FranciaFil: Stuehr, Dennis J.. Lerner Research Institute; Estados UnidosFil: Lamattina, Lorenzo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; ArgentinaFil: Melkonian, Michael. Universitat zu Köln; AlemaniaFil: Tian, Zhijian. BGI Shenzhen; ChinaFil: Zhu, Ying. BGI Shenzhen; ChinaFil: Carpenter, Eric J.. University of Alberta; CanadáFil: Wong, Gane Ka-Shu. University of Alberta; Canadá. BGI Shenzhen; ChinaFil: Wendehenne, David. Centre National de la Recherche Scientifique; Francia. Universite de Bourgogne; FranciaAmerican Association for the Advancement of Science2016-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/56197Jeandroz, Sylvain; Wipf, Daniel; Stuehr, Dennis J.; Lamattina, Lorenzo; Melkonian, Michael; et al.; Occurrence, structure, and evolution of nitric oxide synthase-like proteins in the plant kingdom; American Association for the Advancement of Science; Science Signaling; 9; 417; 3-2016; 1-101945-0877CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1126/scisignal.aad4403info:eu-repo/semantics/altIdentifier/url/http://stke.sciencemag.org/content/9/417/re2info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:00:06Zoai:ri.conicet.gov.ar:11336/56197instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:00:06.526CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Occurrence, structure, and evolution of nitric oxide synthase-like proteins in the plant kingdom
title Occurrence, structure, and evolution of nitric oxide synthase-like proteins in the plant kingdom
spellingShingle Occurrence, structure, and evolution of nitric oxide synthase-like proteins in the plant kingdom
Jeandroz, Sylvain
Nitric Oxide
Nitric Oxide Synthase
Plantae
Evolution
title_short Occurrence, structure, and evolution of nitric oxide synthase-like proteins in the plant kingdom
title_full Occurrence, structure, and evolution of nitric oxide synthase-like proteins in the plant kingdom
title_fullStr Occurrence, structure, and evolution of nitric oxide synthase-like proteins in the plant kingdom
title_full_unstemmed Occurrence, structure, and evolution of nitric oxide synthase-like proteins in the plant kingdom
title_sort Occurrence, structure, and evolution of nitric oxide synthase-like proteins in the plant kingdom
dc.creator.none.fl_str_mv Jeandroz, Sylvain
Wipf, Daniel
Stuehr, Dennis J.
Lamattina, Lorenzo
Melkonian, Michael
Tian, Zhijian
Zhu, Ying
Carpenter, Eric J.
Wong, Gane Ka-Shu
Wendehenne, David
author Jeandroz, Sylvain
author_facet Jeandroz, Sylvain
Wipf, Daniel
Stuehr, Dennis J.
Lamattina, Lorenzo
Melkonian, Michael
Tian, Zhijian
Zhu, Ying
Carpenter, Eric J.
Wong, Gane Ka-Shu
Wendehenne, David
author_role author
author2 Wipf, Daniel
Stuehr, Dennis J.
Lamattina, Lorenzo
Melkonian, Michael
Tian, Zhijian
Zhu, Ying
Carpenter, Eric J.
Wong, Gane Ka-Shu
Wendehenne, David
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Nitric Oxide
Nitric Oxide Synthase
Plantae
Evolution
topic Nitric Oxide
Nitric Oxide Synthase
Plantae
Evolution
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Nitric oxide (NO) signaling regulates various physiological processes in both animals and plants. In animals, NO synthesis is mainly catalyzed by NO synthase (NOS) enzymes. Although NOS-like activities that are sensitive to mammalian NOS inhibitors have been detected in plant extracts, few bona fide plant NOS enzymes have been identified. We searched the data set produced by the 1000 Plants (1KP) international consortium for the presence of transcripts encoding NOS-like proteins in over 1000 species of land plants and algae. We also searched for genes encoding NOS-like enzymes in 24 publicly available algal genomes. We identified no typical NOS sequences in 1087 sequenced transcriptomes of land plants. In contrast, we identified NOS-like sequences in 15 of the 265 algal species analyzed. Even if the presence of NOS enzymes assembled from multipolypeptides in plants cannot be conclusively discarded, the emerging data suggest that, instead of generating NO with evolutionarily conserved NOS enzymes, land plants have evolved finely regulated nitrate assimilation and reduction processes to synthesize NO through a mechanism different than that in animals.
Fil: Jeandroz, Sylvain. AgroSup Dijon; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Wipf, Daniel. Universite de Bourgogne; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Stuehr, Dennis J.. Lerner Research Institute; Estados Unidos
Fil: Lamattina, Lorenzo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: Melkonian, Michael. Universitat zu Köln; Alemania
Fil: Tian, Zhijian. BGI Shenzhen; China
Fil: Zhu, Ying. BGI Shenzhen; China
Fil: Carpenter, Eric J.. University of Alberta; Canadá
Fil: Wong, Gane Ka-Shu. University of Alberta; Canadá. BGI Shenzhen; China
Fil: Wendehenne, David. Centre National de la Recherche Scientifique; Francia. Universite de Bourgogne; Francia
description Nitric oxide (NO) signaling regulates various physiological processes in both animals and plants. In animals, NO synthesis is mainly catalyzed by NO synthase (NOS) enzymes. Although NOS-like activities that are sensitive to mammalian NOS inhibitors have been detected in plant extracts, few bona fide plant NOS enzymes have been identified. We searched the data set produced by the 1000 Plants (1KP) international consortium for the presence of transcripts encoding NOS-like proteins in over 1000 species of land plants and algae. We also searched for genes encoding NOS-like enzymes in 24 publicly available algal genomes. We identified no typical NOS sequences in 1087 sequenced transcriptomes of land plants. In contrast, we identified NOS-like sequences in 15 of the 265 algal species analyzed. Even if the presence of NOS enzymes assembled from multipolypeptides in plants cannot be conclusively discarded, the emerging data suggest that, instead of generating NO with evolutionarily conserved NOS enzymes, land plants have evolved finely regulated nitrate assimilation and reduction processes to synthesize NO through a mechanism different than that in animals.
publishDate 2016
dc.date.none.fl_str_mv 2016-03
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/56197
Jeandroz, Sylvain; Wipf, Daniel; Stuehr, Dennis J.; Lamattina, Lorenzo; Melkonian, Michael; et al.; Occurrence, structure, and evolution of nitric oxide synthase-like proteins in the plant kingdom; American Association for the Advancement of Science; Science Signaling; 9; 417; 3-2016; 1-10
1945-0877
CONICET Digital
CONICET
url http://hdl.handle.net/11336/56197
identifier_str_mv Jeandroz, Sylvain; Wipf, Daniel; Stuehr, Dennis J.; Lamattina, Lorenzo; Melkonian, Michael; et al.; Occurrence, structure, and evolution of nitric oxide synthase-like proteins in the plant kingdom; American Association for the Advancement of Science; Science Signaling; 9; 417; 3-2016; 1-10
1945-0877
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1126/scisignal.aad4403
info:eu-repo/semantics/altIdentifier/url/http://stke.sciencemag.org/content/9/417/re2
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Association for the Advancement of Science
publisher.none.fl_str_mv American Association for the Advancement of Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1842269619800244224
score 13.13397

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