Analysis of Two Polyhydroxyalkanoate Synthases in Bradyrhizobium japonicum USDA 110

Autores
Quelas, Juan Ignacio; Mongiardini, Elias Javier; Pérez Giménez, Julieta; Parisi, Gustavo Daniel; Lodeiro, Anibal
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Bradyrhizobium japonicum USDA 110 has five polyhydroxyalkanoate (PHA) synthases (PhaC) annotated in its genome: bll4360 (phaC1), bll6073 (phaC2), blr3732 (phaC3), blr2885 (phaC4), and bll4548 (phaC5). All these proteins possess the catalytic triad and conserved amino acid residues of polyester synthases and are distributed into four different PhaC classes. We obtained mutants in each of these paralogs and analyzed phaC gene expression and PHA production in liquid cultures. Despite the genetic redundancy, only phaC1 and phaC2 were expressed at significant rates, while PHA accumulation in stationary-phase cultures was impaired only in the phaC1 mutant. Meanwhile, the phaC2 mutant produced more PHA than the wild type under this condition, and surprisingly, the phaC3 transcript increased in the phaC2 background. A double mutant, the phaC2 phaC3 mutant, consistently accumulated less PHA than the phaC2 mutant. PHA accumulation in nodule bacteroids followed a pattern similar to that seen in liquid cultures, being prevented in the phaC1 mutant and increased in the phaC2 mutant in relation to the level in the wild type. Therefore, we used these mutants, together with a phaC1 phaC2 double mutant, to study the B. japonicum PHA requirements for survival, competition for nodulation, and plant growth promotion. All mutants, as well as the wild type, survived for 60 days in a carbon-free medium, regardless of their initial PHA contents. When competing for nodulation against the wild type in a 1:1 proportion, the phaC1 and phaC1 phaC2 mutants occupied only 13 to 15% of the nodules, while the phaC2 mutant occupied 81%, suggesting that the PHA polymer is required for successful competitiveness. However, the bacteroid content of PHA did not affect the shoot dry weight accumulation.
Fil: Quelas, Juan Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina
Fil: Mongiardini, Elias Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina
Fil: Pérez Giménez, Julieta. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina
Fil: Parisi, Gustavo Daniel. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Lodeiro, Anibal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina
Materia
Polyhydroxyalkanoate Synthases
Bradyrhizobium japonicum
phaC1
phaC2
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:11336/24370
Acceder
id CONICETDig_17767e8374673eb779b3b3385d86ba45
oai_identifier_str oai:ri.conicet.gov.ar:11336/24370
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Analysis of Two Polyhydroxyalkanoate Synthases in Bradyrhizobium japonicum USDA 110Quelas, Juan IgnacioMongiardini, Elias JavierPérez Giménez, JulietaParisi, Gustavo DanielLodeiro, AnibalPolyhydroxyalkanoate SynthasesBradyrhizobium japonicumphaC1phaC2https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Bradyrhizobium japonicum USDA 110 has five polyhydroxyalkanoate (PHA) synthases (PhaC) annotated in its genome: bll4360 (phaC1), bll6073 (phaC2), blr3732 (phaC3), blr2885 (phaC4), and bll4548 (phaC5). All these proteins possess the catalytic triad and conserved amino acid residues of polyester synthases and are distributed into four different PhaC classes. We obtained mutants in each of these paralogs and analyzed phaC gene expression and PHA production in liquid cultures. Despite the genetic redundancy, only phaC1 and phaC2 were expressed at significant rates, while PHA accumulation in stationary-phase cultures was impaired only in the phaC1 mutant. Meanwhile, the phaC2 mutant produced more PHA than the wild type under this condition, and surprisingly, the phaC3 transcript increased in the phaC2 background. A double mutant, the phaC2 phaC3 mutant, consistently accumulated less PHA than the phaC2 mutant. PHA accumulation in nodule bacteroids followed a pattern similar to that seen in liquid cultures, being prevented in the phaC1 mutant and increased in the phaC2 mutant in relation to the level in the wild type. Therefore, we used these mutants, together with a phaC1 phaC2 double mutant, to study the B. japonicum PHA requirements for survival, competition for nodulation, and plant growth promotion. All mutants, as well as the wild type, survived for 60 days in a carbon-free medium, regardless of their initial PHA contents. When competing for nodulation against the wild type in a 1:1 proportion, the phaC1 and phaC1 phaC2 mutants occupied only 13 to 15% of the nodules, while the phaC2 mutant occupied 81%, suggesting that the PHA polymer is required for successful competitiveness. However, the bacteroid content of PHA did not affect the shoot dry weight accumulation.Fil: Quelas, Juan Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; ArgentinaFil: Mongiardini, Elias Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; ArgentinaFil: Pérez Giménez, Julieta. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; ArgentinaFil: Parisi, Gustavo Daniel. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Lodeiro, Anibal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; ArgentinaAmerican Society for Microbiology2013-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/24370Quelas, Juan Ignacio; Mongiardini, Elias Javier; Pérez Giménez, Julieta; Parisi, Gustavo Daniel; Lodeiro, Anibal; Analysis of Two Polyhydroxyalkanoate Synthases in Bradyrhizobium japonicum USDA 110; American Society for Microbiology; Journal Of Bacteriology; 195; 14; 7-2013; 3145-31550021-9193CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1128/JB.02203-12info:eu-repo/semantics/altIdentifier/url/http://jb.asm.org/content/195/14/3145info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:01:19Zoai:ri.conicet.gov.ar:11336/24370instacron: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 10:01:19.554CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Analysis of Two Polyhydroxyalkanoate Synthases in Bradyrhizobium japonicum USDA 110
title Analysis of Two Polyhydroxyalkanoate Synthases in Bradyrhizobium japonicum USDA 110
spellingShingle Analysis of Two Polyhydroxyalkanoate Synthases in Bradyrhizobium japonicum USDA 110
Quelas, Juan Ignacio
Polyhydroxyalkanoate Synthases
Bradyrhizobium japonicum
phaC1
phaC2
title_short Analysis of Two Polyhydroxyalkanoate Synthases in Bradyrhizobium japonicum USDA 110
title_full Analysis of Two Polyhydroxyalkanoate Synthases in Bradyrhizobium japonicum USDA 110
title_fullStr Analysis of Two Polyhydroxyalkanoate Synthases in Bradyrhizobium japonicum USDA 110
title_full_unstemmed Analysis of Two Polyhydroxyalkanoate Synthases in Bradyrhizobium japonicum USDA 110
title_sort Analysis of Two Polyhydroxyalkanoate Synthases in Bradyrhizobium japonicum USDA 110
dc.creator.none.fl_str_mv Quelas, Juan Ignacio
Mongiardini, Elias Javier
Pérez Giménez, Julieta
Parisi, Gustavo Daniel
Lodeiro, Anibal
author Quelas, Juan Ignacio
author_facet Quelas, Juan Ignacio
Mongiardini, Elias Javier
Pérez Giménez, Julieta
Parisi, Gustavo Daniel
Lodeiro, Anibal
author_role author
author2 Mongiardini, Elias Javier
Pérez Giménez, Julieta
Parisi, Gustavo Daniel
Lodeiro, Anibal
author2_role author
author
author
author
dc.subject.none.fl_str_mv Polyhydroxyalkanoate Synthases
Bradyrhizobium japonicum
phaC1
phaC2
topic Polyhydroxyalkanoate Synthases
Bradyrhizobium japonicum
phaC1
phaC2
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Bradyrhizobium japonicum USDA 110 has five polyhydroxyalkanoate (PHA) synthases (PhaC) annotated in its genome: bll4360 (phaC1), bll6073 (phaC2), blr3732 (phaC3), blr2885 (phaC4), and bll4548 (phaC5). All these proteins possess the catalytic triad and conserved amino acid residues of polyester synthases and are distributed into four different PhaC classes. We obtained mutants in each of these paralogs and analyzed phaC gene expression and PHA production in liquid cultures. Despite the genetic redundancy, only phaC1 and phaC2 were expressed at significant rates, while PHA accumulation in stationary-phase cultures was impaired only in the phaC1 mutant. Meanwhile, the phaC2 mutant produced more PHA than the wild type under this condition, and surprisingly, the phaC3 transcript increased in the phaC2 background. A double mutant, the phaC2 phaC3 mutant, consistently accumulated less PHA than the phaC2 mutant. PHA accumulation in nodule bacteroids followed a pattern similar to that seen in liquid cultures, being prevented in the phaC1 mutant and increased in the phaC2 mutant in relation to the level in the wild type. Therefore, we used these mutants, together with a phaC1 phaC2 double mutant, to study the B. japonicum PHA requirements for survival, competition for nodulation, and plant growth promotion. All mutants, as well as the wild type, survived for 60 days in a carbon-free medium, regardless of their initial PHA contents. When competing for nodulation against the wild type in a 1:1 proportion, the phaC1 and phaC1 phaC2 mutants occupied only 13 to 15% of the nodules, while the phaC2 mutant occupied 81%, suggesting that the PHA polymer is required for successful competitiveness. However, the bacteroid content of PHA did not affect the shoot dry weight accumulation.
Fil: Quelas, Juan Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina
Fil: Mongiardini, Elias Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina
Fil: Pérez Giménez, Julieta. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina
Fil: Parisi, Gustavo Daniel. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Lodeiro, Anibal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina
description Bradyrhizobium japonicum USDA 110 has five polyhydroxyalkanoate (PHA) synthases (PhaC) annotated in its genome: bll4360 (phaC1), bll6073 (phaC2), blr3732 (phaC3), blr2885 (phaC4), and bll4548 (phaC5). All these proteins possess the catalytic triad and conserved amino acid residues of polyester synthases and are distributed into four different PhaC classes. We obtained mutants in each of these paralogs and analyzed phaC gene expression and PHA production in liquid cultures. Despite the genetic redundancy, only phaC1 and phaC2 were expressed at significant rates, while PHA accumulation in stationary-phase cultures was impaired only in the phaC1 mutant. Meanwhile, the phaC2 mutant produced more PHA than the wild type under this condition, and surprisingly, the phaC3 transcript increased in the phaC2 background. A double mutant, the phaC2 phaC3 mutant, consistently accumulated less PHA than the phaC2 mutant. PHA accumulation in nodule bacteroids followed a pattern similar to that seen in liquid cultures, being prevented in the phaC1 mutant and increased in the phaC2 mutant in relation to the level in the wild type. Therefore, we used these mutants, together with a phaC1 phaC2 double mutant, to study the B. japonicum PHA requirements for survival, competition for nodulation, and plant growth promotion. All mutants, as well as the wild type, survived for 60 days in a carbon-free medium, regardless of their initial PHA contents. When competing for nodulation against the wild type in a 1:1 proportion, the phaC1 and phaC1 phaC2 mutants occupied only 13 to 15% of the nodules, while the phaC2 mutant occupied 81%, suggesting that the PHA polymer is required for successful competitiveness. However, the bacteroid content of PHA did not affect the shoot dry weight accumulation.
publishDate 2013
dc.date.none.fl_str_mv 2013-07
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/11336/24370
Quelas, Juan Ignacio; Mongiardini, Elias Javier; Pérez Giménez, Julieta; Parisi, Gustavo Daniel; Lodeiro, Anibal; Analysis of Two Polyhydroxyalkanoate Synthases in Bradyrhizobium japonicum USDA 110; American Society for Microbiology; Journal Of Bacteriology; 195; 14; 7-2013; 3145-3155
0021-9193
CONICET Digital
CONICET
url http://hdl.handle.net/11336/24370
identifier_str_mv Quelas, Juan Ignacio; Mongiardini, Elias Javier; Pérez Giménez, Julieta; Parisi, Gustavo Daniel; Lodeiro, Anibal; Analysis of Two Polyhydroxyalkanoate Synthases in Bradyrhizobium japonicum USDA 110; American Society for Microbiology; Journal Of Bacteriology; 195; 14; 7-2013; 3145-3155
0021-9193
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1128/JB.02203-12
info:eu-repo/semantics/altIdentifier/url/http://jb.asm.org/content/195/14/3145
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
application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Society for Microbiology
publisher.none.fl_str_mv American Society for Microbiology
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_ 1842269689574588416
score 13.13397

Publicaciones similares