Document Type
Article
Publication Date
10-30-2008
Department
Chemistry and Biochemistry
School
Mathematics and Natural Sciences
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 CO(2) 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 alpha-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.
Publication Title
PLoS ONE
Volume
3
Issue
10
Recommended Citation
Menon, B.,
Dou, Z.,
Heinhorst, S.,
Shively, J. M.,
Cannon, G. C.
(2008). Halothiobacillus neapolitanus Carboxysomes Sequester Heterologous and Chimeric RubisCO Species. PLoS ONE, 3(10).
Available at: https://aquila.usm.edu/fac_pubs/8967
Comments
Published by PLoS ONE at 10.1371/journal.pone.0003570.