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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]

PMID: 23042035

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