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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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:
Article
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
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author 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.
author_facet 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.
author_sort Erb, Tobias J.
collection PubMed
description 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.
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spelling pubmed-34757402013-05-01 A RubisCO like protein links SAM metabolism with isoprenoid biosynthesis 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. Nat Chem Biol Article 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. 2012-10-07 2012-11 /pmc/articles/PMC3475740/ /pubmed/23042035 http://dx.doi.org/10.1038/nchembio.1087 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
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.
A RubisCO like protein links SAM metabolism with isoprenoid biosynthesis
title A RubisCO like protein links SAM metabolism with isoprenoid biosynthesis
title_full A RubisCO like protein links SAM metabolism with isoprenoid biosynthesis
title_fullStr A RubisCO like protein links SAM metabolism with isoprenoid biosynthesis
title_full_unstemmed A RubisCO like protein links SAM metabolism with isoprenoid biosynthesis
title_short A RubisCO like protein links SAM metabolism with isoprenoid biosynthesis
title_sort rubisco like protein links sam metabolism with isoprenoid biosynthesis
topic Article
url 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
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