Abstract

Many bacteria contain intracellular microcompartments with outer shells that are composed of thousands of protein subunits and interiors that are filled with functionally related enzymes. These microcompartments serve as organelles by sequestering specific metabolic pathways in bacterial cells. The carboxysome, a prototypical bacterial microcompartment that is found in cyanobacteria and some chemoautotrophs, encapsulates ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) and carbonic anhydrase, and thereby enhances carbon fixation by elevating the levels of CO₂ in the vicinity of RuBisCO. Evolutionarily related, but functionally distinct, microcompartments are present in diverse bacteria. Although bacterial microcompartments were first observed more than 40 years ago, a detailed understanding of how they function is only now beginning to emerge.

Author affiliations

1. UCLA Department of Chemistry and Biochemistry, University of California, Berkeley, California 94720, USA.
2. UCLA-DOE Institute of Genomics and Proteomics, University of California, Berkeley, California 94720, USA.
3. US Department of Energy — Joint Genome Institute, University of California, Berkeley, California 94720, USA.
4. Department of Plant and Microbial Biology, University of California, Berkeley, California 94720, USA.
5. Department of Chemistry and Biochemistry, The University of Southern Mississippi, Hattiesburg, Mississippi 39406, USA.
6. Department of Genetics and Biochemistry, Clemson University, Clemson, South Carolina 29634, USA.

Correspondence to: Todd O. Yeates^1,2 Email: yeates@mbi.ucla.edu

Published online 4 August 2008

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