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

Acetyl-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 eukaryote...

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Autores principales: Livieri, Andrea L., Navone, Laura, Marcellin, Esteban, Gramajo, Hugo Cesar, Rodriguez, Eduardo
Formato: article artículo publishedVersion
Lenguaje:Inglés
Publicado: Nature 2021
Materias:
Acyl-CoA Carboxylase
Saccharopolyspora
Malonyl-CoA
De Novo Synthesis
Fatty Acids
Acceso en línea:http://hdl.handle.net/2133/19647
http://hdl.handle.net/2133/19647
Aporte de:
Repositorio Hipermedial de la Universidad Nacional de Rosario (UNR) de Universidad Nacional de Rosario
id I15-R121-2133-19647
record_format dspace
institution Universidad Nacional de Rosario
institution_str I-15
repository_str R-121
collection Repositorio Hipermedial de la Universidad Nacional de Rosario (UNR)
language Inglés
orig_language_str_mv eng
topic Acyl-CoA Carboxylase
Saccharopolyspora
Malonyl-CoA
De Novo Synthesis
Fatty Acids
spellingShingle Acyl-CoA Carboxylase
Saccharopolyspora
Malonyl-CoA
De Novo Synthesis
Fatty Acids
Livieri, Andrea L.
Navone, Laura
Marcellin, Esteban
Gramajo, Hugo Cesar
Rodriguez, Eduardo
A novel multidomain acyl-CoA carboxylase in Saccharopolyspora erythraea provides malonyl-CoA for de novo fatty acid biosynthesis
topic_facet Acyl-CoA Carboxylase
Saccharopolyspora
Malonyl-CoA
De Novo Synthesis
Fatty Acids
description Acetyl-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.
format article
artículo
publishedVersion
author Livieri, Andrea L.
Navone, Laura
Marcellin, Esteban
Gramajo, Hugo Cesar
Rodriguez, Eduardo
author_facet Livieri, Andrea L.
Navone, Laura
Marcellin, Esteban
Gramajo, Hugo Cesar
Rodriguez, Eduardo
author_sort Livieri, Andrea L.
title A novel multidomain acyl-CoA carboxylase in Saccharopolyspora erythraea provides malonyl-CoA for de novo fatty acid biosynthesis
title_short A novel multidomain acyl-CoA carboxylase in Saccharopolyspora erythraea provides malonyl-CoA for de novo fatty acid biosynthesis
title_full A novel multidomain acyl-CoA carboxylase in Saccharopolyspora erythraea provides malonyl-CoA for de novo fatty acid biosynthesis
title_fullStr A novel multidomain acyl-CoA carboxylase in Saccharopolyspora erythraea provides malonyl-CoA for de novo fatty acid biosynthesis
title_full_unstemmed A novel multidomain acyl-CoA carboxylase in Saccharopolyspora erythraea provides malonyl-CoA for de novo fatty acid biosynthesis
title_sort novel multidomain acyl-coa carboxylase in saccharopolyspora erythraea provides malonyl-coa for de novo fatty acid biosynthesis
publisher Nature
publishDate 2021
url http://hdl.handle.net/2133/19647
http://hdl.handle.net/2133/19647
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