Label-free and redox proteomic analyses of the triacylglycerol-accumulating Rhodococcus jostii RHA1

Autores
Dávila Costa, José Sebastián; Herrero, O. Marisa; Alvarez, Hector Manuel; Leichert, Lars
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The bacterium Rhodococcus jostii RHA1 synthesizes large amounts of triacylglycerols (TAG) under conditions of nitrogen starvation. To better understand the molecular mechanisms behind this process, we performed proteomic studies in this oleaginous bacterium. Upon nitrogen starvation, we observed a re-routing of the carbon flux towards the formation of TAG. Under these conditions, the cellular lipid content made up more than half of the cell?s dry weight. On the proteome level, this coincided with a shift towards non-glycolytic carbohydrate-metabolizing pathways. These pathways (Entner-Doudoroff and pentose-phosphate shunt) contribute NADPH and precursors of glycerol-3-phosphate and acetyl-CoA to lipogenesis. The expression of proteins involved in the degradation of branched-chain-amino acids and the methyl malonyl-CoA pathway probably provided propionyl-CoA for the biosynthesis of odd-numbered fatty acids, which make up almost 30% of RHA1 fatty acid composition. Additionally, lipolytic and glycerol-degrading enzymes increased in abundance, suggesting a dynamic cycling of cellular lipids. Conversely, abundance of proteins involved in consuming intermediates of lipogenesis decreased. Furthermore, we identified another level of lipogenesis regulation through redox-mediated thiol modification in R. jostii. Enzymes affected included acetyl-CoA carboxylase and a β-ketoacyl-[ACP] synthase II (FabF). An integrative metabolic model for the oleaginous RHA1 strain is proposed based on our results.
Fil: Dávila Costa, José Sebastián. Universidad Nacional de la Patagonia "San Juan Bosco"; Argentina
Fil: Herrero, O. Marisa. Universidad Nacional de la Patagonia "san Juan Bosco". Facultad de Ciencias Naturales - Sede Comodoro; Argentina
Fil: Alvarez, Hector Manuel. Universidad Nacional de la Patagonia "san Juan Bosco". Facultad de Ciencias Naturales - Sede Comodoro; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Nacional Patagónico; Argentina
Fil: Leichert, Lars. Ruhr-Universitat Bochum; Alemania
Materia
Proteome
Rhodococcus
Triacylglycerols
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:11336/5624

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network_name_str CONICET Digital (CONICET)
spelling Label-free and redox proteomic analyses of the triacylglycerol-accumulating Rhodococcus jostii RHA1Dávila Costa, José SebastiánHerrero, O. MarisaAlvarez, Hector ManuelLeichert, LarsProteomeRhodococcusTriacylglycerolshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The bacterium Rhodococcus jostii RHA1 synthesizes large amounts of triacylglycerols (TAG) under conditions of nitrogen starvation. To better understand the molecular mechanisms behind this process, we performed proteomic studies in this oleaginous bacterium. Upon nitrogen starvation, we observed a re-routing of the carbon flux towards the formation of TAG. Under these conditions, the cellular lipid content made up more than half of the cell?s dry weight. On the proteome level, this coincided with a shift towards non-glycolytic carbohydrate-metabolizing pathways. These pathways (Entner-Doudoroff and pentose-phosphate shunt) contribute NADPH and precursors of glycerol-3-phosphate and acetyl-CoA to lipogenesis. The expression of proteins involved in the degradation of branched-chain-amino acids and the methyl malonyl-CoA pathway probably provided propionyl-CoA for the biosynthesis of odd-numbered fatty acids, which make up almost 30% of RHA1 fatty acid composition. Additionally, lipolytic and glycerol-degrading enzymes increased in abundance, suggesting a dynamic cycling of cellular lipids. Conversely, abundance of proteins involved in consuming intermediates of lipogenesis decreased. Furthermore, we identified another level of lipogenesis regulation through redox-mediated thiol modification in R. jostii. Enzymes affected included acetyl-CoA carboxylase and a β-ketoacyl-[ACP] synthase II (FabF). An integrative metabolic model for the oleaginous RHA1 strain is proposed based on our results.Fil: Dávila Costa, José Sebastián. Universidad Nacional de la Patagonia "San Juan Bosco"; ArgentinaFil: Herrero, O. Marisa. Universidad Nacional de la Patagonia "san Juan Bosco". Facultad de Ciencias Naturales - Sede Comodoro; ArgentinaFil: Alvarez, Hector Manuel. Universidad Nacional de la Patagonia "san Juan Bosco". Facultad de Ciencias Naturales - Sede Comodoro; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Nacional Patagónico; ArgentinaFil: Leichert, Lars. Ruhr-Universitat Bochum; AlemaniaMicrobiology Society2015-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/5624Dávila Costa, José Sebastián; Herrero, O. Marisa; Alvarez, Hector Manuel; Leichert, Lars; Label-free and redox proteomic analyses of the triacylglycerol-accumulating Rhodococcus jostii RHA1; Microbiology Society; Microbiology-uk; 161; 2-2015; 593-6101350-0872enginfo:eu-repo/semantics/altIdentifier/url/http://mic.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.000028info:eu-repo/semantics/altIdentifier/doi/info:eu-repo/semantics/altIdentifier/doi/10.1099/mic.0.000028info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:52:59Zoai:ri.conicet.gov.ar:11336/5624instacron: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 09:52:59.86CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Label-free and redox proteomic analyses of the triacylglycerol-accumulating Rhodococcus jostii RHA1
title Label-free and redox proteomic analyses of the triacylglycerol-accumulating Rhodococcus jostii RHA1
spellingShingle Label-free and redox proteomic analyses of the triacylglycerol-accumulating Rhodococcus jostii RHA1
Dávila Costa, José Sebastián
Proteome
Rhodococcus
Triacylglycerols
title_short Label-free and redox proteomic analyses of the triacylglycerol-accumulating Rhodococcus jostii RHA1
title_full Label-free and redox proteomic analyses of the triacylglycerol-accumulating Rhodococcus jostii RHA1
title_fullStr Label-free and redox proteomic analyses of the triacylglycerol-accumulating Rhodococcus jostii RHA1
title_full_unstemmed Label-free and redox proteomic analyses of the triacylglycerol-accumulating Rhodococcus jostii RHA1
title_sort Label-free and redox proteomic analyses of the triacylglycerol-accumulating Rhodococcus jostii RHA1
dc.creator.none.fl_str_mv Dávila Costa, José Sebastián
Herrero, O. Marisa
Alvarez, Hector Manuel
Leichert, Lars
author Dávila Costa, José Sebastián
author_facet Dávila Costa, José Sebastián
Herrero, O. Marisa
Alvarez, Hector Manuel
Leichert, Lars
author_role author
author2 Herrero, O. Marisa
Alvarez, Hector Manuel
Leichert, Lars
author2_role author
author
author
dc.subject.none.fl_str_mv Proteome
Rhodococcus
Triacylglycerols
topic Proteome
Rhodococcus
Triacylglycerols
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The bacterium Rhodococcus jostii RHA1 synthesizes large amounts of triacylglycerols (TAG) under conditions of nitrogen starvation. To better understand the molecular mechanisms behind this process, we performed proteomic studies in this oleaginous bacterium. Upon nitrogen starvation, we observed a re-routing of the carbon flux towards the formation of TAG. Under these conditions, the cellular lipid content made up more than half of the cell?s dry weight. On the proteome level, this coincided with a shift towards non-glycolytic carbohydrate-metabolizing pathways. These pathways (Entner-Doudoroff and pentose-phosphate shunt) contribute NADPH and precursors of glycerol-3-phosphate and acetyl-CoA to lipogenesis. The expression of proteins involved in the degradation of branched-chain-amino acids and the methyl malonyl-CoA pathway probably provided propionyl-CoA for the biosynthesis of odd-numbered fatty acids, which make up almost 30% of RHA1 fatty acid composition. Additionally, lipolytic and glycerol-degrading enzymes increased in abundance, suggesting a dynamic cycling of cellular lipids. Conversely, abundance of proteins involved in consuming intermediates of lipogenesis decreased. Furthermore, we identified another level of lipogenesis regulation through redox-mediated thiol modification in R. jostii. Enzymes affected included acetyl-CoA carboxylase and a β-ketoacyl-[ACP] synthase II (FabF). An integrative metabolic model for the oleaginous RHA1 strain is proposed based on our results.
Fil: Dávila Costa, José Sebastián. Universidad Nacional de la Patagonia "San Juan Bosco"; Argentina
Fil: Herrero, O. Marisa. Universidad Nacional de la Patagonia "san Juan Bosco". Facultad de Ciencias Naturales - Sede Comodoro; Argentina
Fil: Alvarez, Hector Manuel. Universidad Nacional de la Patagonia "san Juan Bosco". Facultad de Ciencias Naturales - Sede Comodoro; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Nacional Patagónico; Argentina
Fil: Leichert, Lars. Ruhr-Universitat Bochum; Alemania
description The bacterium Rhodococcus jostii RHA1 synthesizes large amounts of triacylglycerols (TAG) under conditions of nitrogen starvation. To better understand the molecular mechanisms behind this process, we performed proteomic studies in this oleaginous bacterium. Upon nitrogen starvation, we observed a re-routing of the carbon flux towards the formation of TAG. Under these conditions, the cellular lipid content made up more than half of the cell?s dry weight. On the proteome level, this coincided with a shift towards non-glycolytic carbohydrate-metabolizing pathways. These pathways (Entner-Doudoroff and pentose-phosphate shunt) contribute NADPH and precursors of glycerol-3-phosphate and acetyl-CoA to lipogenesis. The expression of proteins involved in the degradation of branched-chain-amino acids and the methyl malonyl-CoA pathway probably provided propionyl-CoA for the biosynthesis of odd-numbered fatty acids, which make up almost 30% of RHA1 fatty acid composition. Additionally, lipolytic and glycerol-degrading enzymes increased in abundance, suggesting a dynamic cycling of cellular lipids. Conversely, abundance of proteins involved in consuming intermediates of lipogenesis decreased. Furthermore, we identified another level of lipogenesis regulation through redox-mediated thiol modification in R. jostii. Enzymes affected included acetyl-CoA carboxylase and a β-ketoacyl-[ACP] synthase II (FabF). An integrative metabolic model for the oleaginous RHA1 strain is proposed based on our results.
publishDate 2015
dc.date.none.fl_str_mv 2015-02
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/11336/5624
Dávila Costa, José Sebastián; Herrero, O. Marisa; Alvarez, Hector Manuel; Leichert, Lars; Label-free and redox proteomic analyses of the triacylglycerol-accumulating Rhodococcus jostii RHA1; Microbiology Society; Microbiology-uk; 161; 2-2015; 593-610
1350-0872
url http://hdl.handle.net/11336/5624
identifier_str_mv Dávila Costa, José Sebastián; Herrero, O. Marisa; Alvarez, Hector Manuel; Leichert, Lars; Label-free and redox proteomic analyses of the triacylglycerol-accumulating Rhodococcus jostii RHA1; Microbiology Society; Microbiology-uk; 161; 2-2015; 593-610
1350-0872
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://mic.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.000028
info:eu-repo/semantics/altIdentifier/doi/
info:eu-repo/semantics/altIdentifier/doi/10.1099/mic.0.000028
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 Microbiology Society
publisher.none.fl_str_mv Microbiology Society
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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