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A Guanidine-Degrading Enzyme Controls Genomic Stability of Ethylene-Producing Cyanobacteria

Journal Article · · Nature Communications
 [1];  [2];  [3];  [3];  [2];  [2];  [4]
  1. National Renewable Energy Lab. (NREL), Golden, CO (United States). Biosciences Center; Vanderbilt Univ., Nashville, TN (United States)
  2. Vanderbilt Univ., Nashville, TN (United States)
  3. Texas A & M Univ., College Station, TX (United States). Synthetic and Systems Biology Innovation Hub
  4. National Renewable Energy Lab. (NREL), Golden, CO (United States). Biosciences Center
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.
Research Organization:
National Renewable Energy Laboratory (NREL), Golden, CO (United States)
Sponsoring Organization:
National Institutes of Health (NIH); USDOE Office of Energy Efficiency and Renewable Energy (EERE), Bioenergy Technologies Office
Grant/Contract Number:
AC36-08GO28308; AR0000203; SC0018344; SC0019388; SC0019404
OSTI ID:
1819078
Report Number(s):
NREL/JA--2700-79641; MainId:35862; UUID:b8d5d784-4bc7-4c56-b0e1-dc16e3299570; MainAdminID:61709
Journal Information:
Nature Communications, Journal Name: Nature Communications Vol. 12; ISSN 2041-1723
Publisher:
Nature Publishing GroupCopyright Statement
Country of Publication:
United States
Language:
English

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