Challenges to develop nitrogen-fixing cereals by direct nif-gene transfer

Autores
Curatti, Leonardo; Rubio, Luis M.
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Some regions of the developing world suffer low cereal production yields due to low fertilizer inputs, among other factors. Biological N2 fixation, catalyzed by the prokaryotic enzyme nitrogenase, is an alternative to the use of synthetic N fertilizers. The molybdenum nitrogenase is an O2-labile metalloenzyme composed of the NifDK and NifH proteins, which biosyntheses require a number of nif gene products. A challenging strategy to increase cereal crop productivity in a scenario of low N fertilization is the direct transfer of nif genes into cereals. The sensitivity of nitrogenase to O2 and the apparent complexity of nitrogenase biosynthesis are the main barriers identified so far. Expression of active NifH requires the products of nifM, nifH, and possibly nifU and nifS, whereas active NifDK requires the products of nifH, nifD, nifK, nifB, nifE, nifN, and possibly nifU, nifS, nifQ, nifV, nafY, nifW and nifZ. Plastids and mitochondria are potential subcellular locations for nitrogenase. Both could provide the ATP and electrons required for nitrogenase to function but they differ in their internal O2 levels and their ability to incorporate ammonium into amino acids.
Fil: Curatti, Leonardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones En Biodiversidad y Biotecnología; Argentina. Fundación para Investigaciones Biológicas Aplicadas; España
Fil: Rubio, Luis M.. Universidad Politecnica de Madrid; España
Materia
Cereales
Nitrogen Fixation
Genetic Engineering
Fertilizers
Food Security
Nitrogenase
Nif
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/10744

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spelling Challenges to develop nitrogen-fixing cereals by direct nif-gene transferCuratti, LeonardoRubio, Luis M.CerealesNitrogen FixationGenetic EngineeringFertilizersFood SecurityNitrogenaseNifhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Some regions of the developing world suffer low cereal production yields due to low fertilizer inputs, among other factors. Biological N2 fixation, catalyzed by the prokaryotic enzyme nitrogenase, is an alternative to the use of synthetic N fertilizers. The molybdenum nitrogenase is an O2-labile metalloenzyme composed of the NifDK and NifH proteins, which biosyntheses require a number of nif gene products. A challenging strategy to increase cereal crop productivity in a scenario of low N fertilization is the direct transfer of nif genes into cereals. The sensitivity of nitrogenase to O2 and the apparent complexity of nitrogenase biosynthesis are the main barriers identified so far. Expression of active NifH requires the products of nifM, nifH, and possibly nifU and nifS, whereas active NifDK requires the products of nifH, nifD, nifK, nifB, nifE, nifN, and possibly nifU, nifS, nifQ, nifV, nafY, nifW and nifZ. Plastids and mitochondria are potential subcellular locations for nitrogenase. Both could provide the ATP and electrons required for nitrogenase to function but they differ in their internal O2 levels and their ability to incorporate ammonium into amino acids.Fil: Curatti, Leonardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones En Biodiversidad y Biotecnología; Argentina. Fundación para Investigaciones Biológicas Aplicadas; EspañaFil: Rubio, Luis M.. Universidad Politecnica de Madrid; EspañaElsevier Ireland2014-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/10744Curatti, Leonardo; Rubio, Luis M.; Challenges to develop nitrogen-fixing cereals by direct nif-gene transfer; Elsevier Ireland; Plant Science; 225; 8-2014; 130–1370168-9452enginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.plantsci.2014.06.003info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S016894521400137Xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:34:45Zoai:ri.conicet.gov.ar:11336/10744instacron: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:34982025-09-29 10:34:45.412CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Challenges to develop nitrogen-fixing cereals by direct nif-gene transfer
title Challenges to develop nitrogen-fixing cereals by direct nif-gene transfer
spellingShingle Challenges to develop nitrogen-fixing cereals by direct nif-gene transfer
Curatti, Leonardo
Cereales
Nitrogen Fixation
Genetic Engineering
Fertilizers
Food Security
Nitrogenase
Nif
title_short Challenges to develop nitrogen-fixing cereals by direct nif-gene transfer
title_full Challenges to develop nitrogen-fixing cereals by direct nif-gene transfer
title_fullStr Challenges to develop nitrogen-fixing cereals by direct nif-gene transfer
title_full_unstemmed Challenges to develop nitrogen-fixing cereals by direct nif-gene transfer
title_sort Challenges to develop nitrogen-fixing cereals by direct nif-gene transfer
dc.creator.none.fl_str_mv Curatti, Leonardo
Rubio, Luis M.
author Curatti, Leonardo
author_facet Curatti, Leonardo
Rubio, Luis M.
author_role author
author2 Rubio, Luis M.
author2_role author
dc.subject.none.fl_str_mv Cereales
Nitrogen Fixation
Genetic Engineering
Fertilizers
Food Security
Nitrogenase
Nif
topic Cereales
Nitrogen Fixation
Genetic Engineering
Fertilizers
Food Security
Nitrogenase
Nif
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Some regions of the developing world suffer low cereal production yields due to low fertilizer inputs, among other factors. Biological N2 fixation, catalyzed by the prokaryotic enzyme nitrogenase, is an alternative to the use of synthetic N fertilizers. The molybdenum nitrogenase is an O2-labile metalloenzyme composed of the NifDK and NifH proteins, which biosyntheses require a number of nif gene products. A challenging strategy to increase cereal crop productivity in a scenario of low N fertilization is the direct transfer of nif genes into cereals. The sensitivity of nitrogenase to O2 and the apparent complexity of nitrogenase biosynthesis are the main barriers identified so far. Expression of active NifH requires the products of nifM, nifH, and possibly nifU and nifS, whereas active NifDK requires the products of nifH, nifD, nifK, nifB, nifE, nifN, and possibly nifU, nifS, nifQ, nifV, nafY, nifW and nifZ. Plastids and mitochondria are potential subcellular locations for nitrogenase. Both could provide the ATP and electrons required for nitrogenase to function but they differ in their internal O2 levels and their ability to incorporate ammonium into amino acids.
Fil: Curatti, Leonardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones En Biodiversidad y Biotecnología; Argentina. Fundación para Investigaciones Biológicas Aplicadas; España
Fil: Rubio, Luis M.. Universidad Politecnica de Madrid; España
description Some regions of the developing world suffer low cereal production yields due to low fertilizer inputs, among other factors. Biological N2 fixation, catalyzed by the prokaryotic enzyme nitrogenase, is an alternative to the use of synthetic N fertilizers. The molybdenum nitrogenase is an O2-labile metalloenzyme composed of the NifDK and NifH proteins, which biosyntheses require a number of nif gene products. A challenging strategy to increase cereal crop productivity in a scenario of low N fertilization is the direct transfer of nif genes into cereals. The sensitivity of nitrogenase to O2 and the apparent complexity of nitrogenase biosynthesis are the main barriers identified so far. Expression of active NifH requires the products of nifM, nifH, and possibly nifU and nifS, whereas active NifDK requires the products of nifH, nifD, nifK, nifB, nifE, nifN, and possibly nifU, nifS, nifQ, nifV, nafY, nifW and nifZ. Plastids and mitochondria are potential subcellular locations for nitrogenase. Both could provide the ATP and electrons required for nitrogenase to function but they differ in their internal O2 levels and their ability to incorporate ammonium into amino acids.
publishDate 2014
dc.date.none.fl_str_mv 2014-08
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/11336/10744
Curatti, Leonardo; Rubio, Luis M.; Challenges to develop nitrogen-fixing cereals by direct nif-gene transfer; Elsevier Ireland; Plant Science; 225; 8-2014; 130–137
0168-9452
url http://hdl.handle.net/11336/10744
identifier_str_mv Curatti, Leonardo; Rubio, Luis M.; Challenges to develop nitrogen-fixing cereals by direct nif-gene transfer; Elsevier Ireland; Plant Science; 225; 8-2014; 130–137
0168-9452
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.plantsci.2014.06.003
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S016894521400137X
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Ireland
publisher.none.fl_str_mv Elsevier Ireland
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
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