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Halothiobacillus neapolitanus Carboxysomes Sequester Heterologous and Chimeric RubisCO Species

Authors
Publisher
Public Library of Science
Publication Date
Volume
3
Issue
10
Identifiers
DOI: 10.1371/journal.pone.0003570
Keywords
  • Research Article
  • Biochemistry/Macromolecular Assemblies And Machines
  • Microbiology/Microbial Growth And Development
  • Microbiology/Microbial Physiology And Metabolism
Disciplines
  • Biology
  • Engineering
  • Physics

Abstract

Background The carboxysome is a bacterial microcompartment that consists of a polyhedral protein shell filled with ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO), the enzyme that catalyzes the first step of CO2 fixation via the Calvin-Benson-Bassham cycle. Methodology/Principal Findings To analyze the role of RubisCO in carboxysome biogenesis in vivo we have created a series of Halothiobacillus neapolitanus RubisCO mutants. We identified the large subunit of the enzyme as an important determinant for its sequestration into α-carboxysomes and found that the carboxysomes of H. neapolitanus readily incorporate chimeric and heterologous RubisCO species. Intriguingly, a mutant lacking carboxysomal RubisCO assembles empty carboxysome shells of apparently normal shape and composition. Conclusions/Significance These results indicate that carboxysome shell architecture is not determined by the enzyme they normally sequester. Our study provides, for the first time, clear evidence that carboxysome contents can be manipulated and suggests future nanotechnological applications that are based upon engineered protein microcompartments.

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