A RubisCO-like protein links SAM metabolism with isoprenoid biosynthesis

Tobias J. Erb, Bradley S. Evans, Kyuil Cho, Benjamin P. Warlick, Jaya Sriram, B. Mc Kay Wood, Heidi J. Imker, Jonathan V. Sweedler, F. Robert Tabita, John A. Gerlt

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)926-932
Number of pages7
JournalNature chemical biology
Volume8
Issue number11
DOIs
StatePublished - Nov 2012

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ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Erb, T. J., Evans, B. S., Cho, K., Warlick, B. P., Sriram, J., Wood, B. M. K., Imker, H. J., Sweedler, J. V., Tabita, F. R., & Gerlt, J. A. (2012). A RubisCO-like protein links SAM metabolism with isoprenoid biosynthesis. Nature chemical biology, 8(11), 926-932. https://doi.org/10.1038/nchembio.1087