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A guanidine-degrading enzyme controls genomic stability of ethylene-producing cyanobacteria

Author

Listed:
  • Bo Wang

    (National Renewable Energy Laboratory
    Vanderbilt University)

  • Yao Xu

    (Vanderbilt University)

  • Xin Wang

    (Texas A&M University
    Miami University)

  • Joshua S. Yuan

    (Texas A&M University)

  • Carl H. Johnson

    (Vanderbilt University)

  • Jamey D. Young

    (Vanderbilt University
    Vanderbilt University)

  • Jianping Yu

    (National Renewable Energy Laboratory)

Abstract

Recent studies have revealed the prevalence and biological significance of guanidine metabolism in nature. However, the metabolic pathways used by microbes to degrade guanidine or mitigate its toxicity have not been widely studied. Here, via comparative proteomics and subsequent experimental validation, we demonstrate that Sll1077, previously annotated as an agmatinase enzyme in the model cyanobacterium Synechocystis sp. PCC 6803, is more likely a guanidinase as it can break down guanidine rather than agmatine into urea and ammonium. The model cyanobacterium Synechococcus elongatus PCC 7942 strain engineered to express the bacterial ethylene-forming enzyme (EFE) exhibits unstable ethylene production due to toxicity and genomic instability induced by accumulation of the EFE-byproduct guanidine. Co-expression of EFE and Sll1077 significantly enhances genomic stability and enables the resulting strain to achieve sustained high-level ethylene production. These findings expand our knowledge of natural guanidine degradation pathways and demonstrate their biotechnological application to support ethylene bioproduction.

Suggested Citation

  • Bo Wang & Yao Xu & Xin Wang & Joshua S. Yuan & Carl H. Johnson & Jamey D. Young & Jianping Yu, 2021. "A guanidine-degrading enzyme controls genomic stability of ethylene-producing cyanobacteria," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-25369-x
    DOI: 10.1038/s41467-021-25369-x
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