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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/10744
Ver los metadatos del registro completo
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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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13.070432 |