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A catalog of the diversity and ubiquity of bacterial microcompartments

Author

Listed:
  • Markus Sutter

    (Lawrence Berkeley National Laboratory
    Michigan State University)

  • Matthew R. Melnicki

    (Michigan State University)

  • Frederik Schulz

    (Lawrence Berkeley National Laboratory)

  • Tanja Woyke

    (Lawrence Berkeley National Laboratory)

  • Cheryl A. Kerfeld

    (Lawrence Berkeley National Laboratory
    Michigan State University
    Michigan State University)

Abstract

Bacterial microcompartments (BMCs) are organelles that segregate segments of metabolic pathways which are incompatible with surrounding metabolism. BMCs consist of a selectively permeable shell, composed of three types of structurally conserved proteins, together with sequestered enzymes that vary among functionally distinct BMCs. Genes encoding shell proteins are typically clustered with those for the encapsulated enzymes. Here, we report that the number of identifiable BMC loci has increased twenty-fold since the last comprehensive census of 2014, and the number of distinct BMC types has doubled. The new BMC types expand the range of compartmentalized catalysis and suggest that there is more BMC biochemistry yet to be discovered. Our comprehensive catalog of BMCs provides a framework for their identification, correlation with bacterial niche adaptation, experimental characterization, and development of BMC-based nanoarchitectures for biomedical and bioengineering applications.

Suggested Citation

  • Markus Sutter & Matthew R. Melnicki & Frederik Schulz & Tanja Woyke & Cheryl A. Kerfeld, 2021. "A catalog of the diversity and ubiquity of bacterial microcompartments," Nature Communications, Nature, vol. 12(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-24126-4
    DOI: 10.1038/s41467-021-24126-4
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    Cited by:

    1. Tao Ni & Yaqi Sun & Will Burn & Monsour M. J. Al-Hazeem & Yanan Zhu & Xiulian Yu & Lu-Ning Liu & Peijun Zhang, 2022. "Structure and assembly of cargo Rubisco in two native α-carboxysomes," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    2. Carolyn E. Mills & Curt Waltmann & Andre G. Archer & Nolan W. Kennedy & Charlotte H. Abrahamson & Alexander D. Jackson & Eric W. Roth & Sasha Shirman & Michael C. Jewett & Niall M. Mangan & Monica Olv, 2022. "Vertex protein PduN tunes encapsulated pathway performance by dictating bacterial metabolosome morphology," Nature Communications, Nature, vol. 13(1), pages 1-13, December.

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