Location: Natural Products Utilization ResearchTitle: The contribution of Romidepsin to the herbicidal activity of Burkholderia rinojensis biopesticide
|OWENS, DANIEL - University Of Hawaii|
|Bajsa Hirschel, Joanna|
|CARBONARI, CAIO - Sao Paulo State University (UNESP)|
|GOMES, GIOVANNA - Sao Paulo State University (UNESP)|
|ASOLKAR, RATNAKAR - Marrone Bio Innovations|
|BODDY, LOUIS - Marrone Bio Innovations|
|DAYAN, FRANCK - Colorado State University|
Submitted to: Journal of Natural Products
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 2/15/2020
Publication Date: 2/24/2020
Citation: Owens, D.K., Bajsa Hirschel, J.N., Duke, S.O., Carbonari, C.A., Gomes, G.L., Asolkar, R., Boddy, L., Dayan, F.E. 2020. The contribution of Romidepsin to the herbicidal activity of Burkholderia rinojensis biopesticide. Journal of Natural Products. 83(4):843-851. https://doi.org/10.1021/acs.jnatprod.9b00405.
Interpretive Summary: The microbial broth of Burkholderia rinojensis strain A396 is herbicidal to a number of weed species with greater observed efficacy against broadleaf than grass weeds. Romidepsin, which is present in small amounts in the microbial broth, was isolated and purified using standard chromatographic techniques. We established that pure romidepsin is a natural proherbicide that targets the activity of plant histone deacetylases (HDAC).
Technical Abstract: In conclusion, the microbial broth of B. rinojensis strain A396 is herbicidal to a number of weed species, and its efficacy is greater on broadleaf weeds than grass weeds. A portion of this activity is attributed to romidepsin, which is present in small amounts in the microbial broth. We confirmed that romidepsin was a natural proherbicide acting via inhibition of plant histone deacetylases (HDAC) activity, and that its activity was greater when the macrocyclic disulfide bridge was reduced to liberate the highly reactive free butenyl thiol side chain. Molecular dynamic simulation of the binding of reduced form of romidepsin to at HDAC19 indicated that this form of the proherbicide could reach deep inside the catalytic domain and interact with a functional zinc atom of the enzyme.