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Vertex protein PduN tunes encapsulated pathway performance by dictating bacterial metabolosome morphology

Author

Listed:
  • Carolyn E. Mills

    (Northwestern University)

  • Curt Waltmann

    (Northwestern University)

  • Andre G. Archer

    (Northwestern University)

  • Nolan W. Kennedy

    (Northwestern University)

  • Charlotte H. Abrahamson

    (Northwestern University)

  • Alexander D. Jackson

    (Northwestern University)

  • Eric W. Roth

    (Northwestern University Atomic and Nanoscale Characterization Experimental Center)

  • Sasha Shirman

    (Northwestern University)

  • Michael C. Jewett

    (Northwestern University
    Northwestern University)

  • Niall M. Mangan

    (Northwestern University
    Northwestern University
    Northwestern University)

  • Monica Olvera de la Cruz

    (Northwestern University
    Northwestern University
    Northwestern University)

  • Danielle Tullman-Ercek

    (Northwestern University
    Northwestern University)

Abstract

Engineering subcellular organization in microbes shows great promise in addressing bottlenecks in metabolic engineering efforts; however, rules guiding selection of an organization strategy or platform are lacking. Here, we study compartment morphology as a factor in mediating encapsulated pathway performance. Using the 1,2-propanediol utilization microcompartment (Pdu MCP) system from Salmonella enterica serovar Typhimurium LT2, we find that we can shift the morphology of this protein nanoreactor from polyhedral to tubular by removing vertex protein PduN. Analysis of the metabolic function between these Pdu microtubes (MTs) shows that they provide a diffusional barrier capable of shielding the cytosol from a toxic pathway intermediate, similar to native MCPs. However, kinetic modeling suggests that the different surface area to volume ratios of MCP and MT structures alters encapsulated pathway performance. Finally, we report a microscopy-based assay that permits rapid assessment of Pdu MT formation to enable future engineering efforts on these structures.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-31279-3
    DOI: 10.1038/s41467-022-31279-3
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    References listed on IDEAS

    as
    1. Andrew Hagen & Markus Sutter & Nancy Sloan & Cheryl A. Kerfeld, 2018. "Programmed loading and rapid purification of engineered bacterial microcompartment shells," Nature Communications, Nature, vol. 9(1), pages 1-10, December.
    2. Emily C. Hartman & Christopher M. Jakobson & Andrew H. Favor & Marco J. Lobba & Ester Álvarez-Benedicto & Matthew B. Francis & Danielle Tullman-Ercek, 2018. "Quantitative characterization of all single amino acid variants of a viral capsid-based drug delivery vehicle," Nature Communications, Nature, vol. 9(1), pages 1-11, December.
    3. 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.
    4. Matthew J. Lee & Judith Mantell & Ian R. Brown & Jordan M. Fletcher & Paul Verkade & Richard W. Pickersgill & Derek N. Woolfson & Stefanie Frank & Martin J. Warren, 2018. "De novo targeting to the cytoplasmic and luminal side of bacterial microcompartments," Nature Communications, Nature, vol. 9(1), pages 1-11, December.
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