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A RubisCO-like protein links SAM metabolism with isoprenoid biosynthesis.


ABSTRACT: 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 from Rhodospirillum rubrum. Our studies unraveled an unexpected link in bacterial central carbon metabolism between S-adenosylmethionine-dependent polyamine metabolism and isoprenoid biosynthesis and also provide an alternative approach to assign enzyme function at the organismic level.

SUBMITTER: Erb TJ 

PROVIDER: S-EPMC3475740 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature

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A RubisCO-like protein links SAM metabolism with isoprenoid biosynthesis.

Erb Tobias J TJ   Evans Bradley S BS   Cho Kyuil K   Warlick Benjamin P BP   Sriram Jaya J   Wood B McKay BM   Imker Heidi J HJ   Sweedler Jonathan V JV   Tabita F Robert FR   Gerlt John A JA  

Nature chemical biology 20121007 11


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 from Rhodospirillum rubrum. Our studies unraveled an unexpected link in bacterial central carbon metabolism between S-adenosylmethionine-dependent  ...[more]

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