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A RubisCO like protein links SAM metabolism with isoprenoid biosynthesis

Functional assignment of uncharacterized proteins is a challenge in the era of large-scale genome sequencing. Here, we combine in extracto-NMR, proteomics, and transcriptomics with a newly developed (knock-out) metabolomics platform to determine a potential physiological role for a ribulose-1,5-bisp...

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Detalles Bibliográficos
Autores principales: Erb, Tobias J., Evans, Bradley S., Cho, Kyuil, Warlick, Benjamin P., Sriram, Jaya, Wood, B. McKay, Imker, Heidi J., Sweedler, Jonathan V., Tabita, F. Robert, Gerlt, John A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3475740/
https://www.ncbi.nlm.nih.gov/pubmed/23042035
http://dx.doi.org/10.1038/nchembio.1087
Descripción
Sumario:Functional assignment of uncharacterized proteins is a challenge in the era of large-scale genome sequencing. Here, we combine in extracto-NMR, proteomics, and transcriptomics with a newly developed (knock-out) metabolomics platform to determine a potential physiological role for a ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO)-like protein (RLP) from Rhodospirillum rubrum. Our studies unravelled an unexpected link in bacterial central carbon metabolism between S-adenosylmethionine (SAM)-dependent polyamine metabolism and isoprenoid biosynthesis and also provide an alternative approach to assign enzyme function at the organismic level.