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A novel multidomain acyl-CoA carboxylase in Saccharopolyspora erythraea provides malonyl-CoA for de novo fatty acid biosynthesis

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dc.citation.titleScientific Reportses
dc.citation.volume9es
dc.creatorLivieri, Andrea L.
dc.creatorNavone, Laura
dc.creatorMarcellin, Esteban
dc.creatorGramajo, Hugo Cesar
dc.creatorRodriguez, Eduardo
dc.date.accessioned2021-02-18T23:49:04Z
dc.date.available2021-02-18T23:49:04Z
dc.date.issued2019-04-30
dc.descriptionAcetyl-CoA carboxylases (ACCs) are enzyme complexes generally composed of three catalytic domains and distributed in all organisms. In prokaryotes and plastids of most plants, these domains are encoded in distinct subunits forming heteromeric complexes. Distinctively, cytosolic ACCs from eukaryotes and plastids of graminaceous monocots, are organized in a single multidomain polypeptide. Until now, no multidomain ACCs had been discovered in bacteria. Here, we show that a putative multidomain ACC in Saccharopolyspora erythraea is encoded by the sace_4237 gene, representing the frst prokaryotic ACC homodimeric multidomain complex described. The SACE_4237 complex has both acetyl-CoA and propionyl-CoA carboxylase activities. Importantly, we demonstrate that sace_4237 is essential for S. erythraea survival as determined by the construction of a sace_4237 conditional mutant. Altogether, our results show that this prokaryotic homodimeric multidomain ACC provides malonyl-CoA for de novo fatty acid biosynthesis. Furthermore, the data presented here suggests that evolution of these enzyme complexes, from single domain subunits to eukaryotic multidomain ACCs, occurred in bacteria through domain fusion.es
dc.description.filFil: Livieri, Andrea L. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR -CONICET); Argentina.es
dc.description.filFil: Navone, Laura. University of Queensland. Australian Institute for Bioengineering and Nanotechnology; Australia.es
dc.description.filFil: Navone, Laura. University of Queensland. Science and Engineering Faculty. Molecular Biology & Industrial Biotechnology; Australia.es
dc.description.filFil: Marcellin, Esteban. University of Queensland. Australian Institute for Bioengineering and Nanotechnology; Australia.es
dc.description.filFil: Gramajo, Hugo Cesar. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR -CONICET); Argentina.es
dc.description.sponsorshipAgencia Nacional de Promoción Científica y Tecnológica (ANPCyT): PICT2015-2022 y PICT2017-2421es
dc.formatapplication/pdf
dc.format.extent1-10es
dc.identifier.issn2045-2322es
dc.identifier.urihttp://hdl.handle.net/2133/19647
dc.language.isoenges
dc.publisherNaturees
dc.relation.publisherversionhttps://www.nature.com/articles/s41598-019-43223-5es
dc.relation.publisherversionhttps://doi.org/10.1038/s41598-019-43223-5es
dc.rightsopenAccesses
dc.rights.holderUniversidad Nacional de Rosarioes
dc.rights.holderLivieri, Andrea L.es
dc.rights.holderNavone, Lauraes
dc.rights.holderMarcellin, Estebanes
dc.rights.holderGramajo, Hugo Cesares
dc.rights.holderRodriguez, Eduardoes
dc.rights.textAttribution 4.0 International (CC BY 4.0)es
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/*
dc.subjectAcyl-CoA Carboxylasees
dc.subjectSaccharopolysporaes
dc.subjectMalonyl-CoAes
dc.subjectDe Novo Synthesises
dc.subjectFatty Acidses
dc.titleA novel multidomain acyl-CoA carboxylase in Saccharopolyspora erythraea provides malonyl-CoA for de novo fatty acid biosynthesises
dc.typearticle
dc.typeartículo
dc.typepublishedVersion
dc.type.collectionarticulo
dc.type.versionpublishedVersiones

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