Modularity of a carbon-fixing protein organelle

Walter Bonacci, Poh K. Teng, Bruno Afonso, Henrike Niederholtmeyer, Patricia Grob, Pamela A. Silver, David F. Savage

Research output: Contribution to journalArticlepeer-review

223 Scopus citations

Abstract

Bacterial microcompartments are proteinaceous complexes that catalyze metabolic pathways in a manner reminiscent of organelles. Although microcompartment structure is well understood, much less is known about their assembly and function in vivo. We show here that carboxysomes, CO 2-fixing microcompartments encoded by 10 genes, can be heterologously produced in Escherichia coli. Expression of carboxysomes in E. coli resulted in the production of icosahedral complexes similar to those from the native host. In vivo, the complexes were capable of both assembling with carboxysomal proteins and fixing CO2. Characterization of purified synthetic carboxysomes indicated that they were well formed in structure, contained the expected molecular components, and were capable of fixing CO2 in vitro. In addition, we verify association of the postulated pore-forming protein CsoS1D with the carboxysome and show how it may modulate function. We have developed a genetic system capable of producing modular carbon-fixing microcompartments in a heterologous host. In doing so, we lay the groundwork for understanding these elaborate protein complexes and for the synthetic biological engineering of self-assembling molecular structures.

Original languageEnglish
Pages (from-to)478-483
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume109
Issue number2
DOIs
StatePublished - 10 Jan 2012
Externally publishedYes

Keywords

  • Metabolic engineering
  • Ribulose 1,5-bisphosphate carboxylase/oxygenase
  • Self-assembly
  • Synthetic biology

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