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Acetyl-CoA-mediated activation of Mycobacterium tuberculosis isocitrate lyase 2

Author

Listed:
  • Ram Prasad Bhusal

    (The University of Auckland)

  • Wanting Jiao

    (Victoria University of Wellington
    The University of Auckland)

  • Brooke X. C. Kwai

    (The University of Auckland)

  • Jóhannes Reynisson

    (The University of Auckland
    Keele University)

  • Annabelle J. Collins

    (The University of Auckland)

  • Jonathan Sperry

    (The University of Auckland)

  • Ghader Bashiri

    (The University of Auckland
    The University of Auckland)

  • Ivanhoe K. H. Leung

    (The University of Auckland
    The University of Auckland)

Abstract

Isocitrate lyase is important for lipid utilisation by Mycobacterium tuberculosis but its ICL2 isoform is poorly understood. Here we report that binding of the lipid metabolites acetyl-CoA or propionyl-CoA to ICL2 induces a striking structural rearrangement, substantially increasing isocitrate lyase and methylisocitrate lyase activities. Thus, ICL2 plays a pivotal role regulating carbon flux between the tricarboxylic acid (TCA) cycle, glyoxylate shunt and methylcitrate cycle at high lipid concentrations, a mechanism essential for bacterial growth and virulence.

Suggested Citation

  • Ram Prasad Bhusal & Wanting Jiao & Brooke X. C. Kwai & Jóhannes Reynisson & Annabelle J. Collins & Jonathan Sperry & Ghader Bashiri & Ivanhoe K. H. Leung, 2019. "Acetyl-CoA-mediated activation of Mycobacterium tuberculosis isocitrate lyase 2," Nature Communications, Nature, vol. 10(1), pages 1-7, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-12614-7
    DOI: 10.1038/s41467-019-12614-7
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