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dc.contributor.author
Dávila Costa, José Sebastián
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dc.contributor.author
Herrero, O. Marisa
dc.contributor.author
Alvarez, Hector Manuel
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dc.contributor.author
Leichert, Lars
dc.date.available
2016-05-11T11:56:21Z
dc.date.issued
2015-02
dc.identifier.citation
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
dc.identifier.issn
1350-0872
dc.identifier.uri
http://hdl.handle.net/11336/5624
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Microbiology Society
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Proteome
dc.subject
Rhodococcus
dc.subject
Triacylglycerols
dc.subject.classification
Biología Celular, Microbiología
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Label-free and redox proteomic analyses of the triacylglycerol-accumulating Rhodococcus jostii RHA1
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2016-04-28T14:50:02Z
dc.journal.volume
161
dc.journal.pagination
593-610
dc.journal.pais
Reino Unido
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dc.journal.ciudad
London
dc.description.fil
Fil: Dávila Costa, José Sebastián. Universidad Nacional de la Patagonia "San Juan Bosco"; Argentina
dc.description.fil
Fil: Herrero, O. Marisa. Universidad Nacional de la Patagonia "san Juan Bosco". Facultad de Ciencias Naturales - Sede Comodoro; Argentina
dc.description.fil
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
dc.description.fil
Fil: Leichert, Lars. Ruhr-Universitat Bochum; Alemania
dc.journal.title
Microbiology-uk
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://mic.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.000028
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/10.1099/mic.0.000028
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1099/mic.0.000028
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