A RubisCO-like protein links SAM metabolism with isoprenoid biosynthesis

Nat Chem Biol. 2012 Nov;8(11):926-32. doi: 10.1038/nchembio.1087. Epub 2012 Oct 7.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Deoxyadenosines / chemistry
  • Deoxyadenosines / metabolism
  • Magnetic Resonance Spectroscopy
  • Molecular Structure
  • Polyamines / chemistry
  • Polyamines / metabolism
  • Proteomics
  • Rhodospirillum rubrum / enzymology*
  • Ribulose-Bisphosphate Carboxylase / chemistry
  • Ribulose-Bisphosphate Carboxylase / genetics
  • Ribulose-Bisphosphate Carboxylase / metabolism*
  • S-Adenosylmethionine / chemistry
  • S-Adenosylmethionine / metabolism*
  • Terpenes / chemistry
  • Terpenes / metabolism*
  • Thionucleosides / chemistry
  • Thionucleosides / metabolism
  • Transcriptome / genetics

Substances

  • Deoxyadenosines
  • Polyamines
  • Terpenes
  • Thionucleosides
  • 5'-methylthioadenosine
  • S-Adenosylmethionine
  • Ribulose-Bisphosphate Carboxylase