Characterization of a helminthosporic acid analog that is a selective agonist of gibberellin receptor. Issue 14 (1st August 2018)

• Record Type: Journal Article
• Authors: Miyazaki, Sho; Tomita, Kenji; Yamane, Hisakazu; Kobayashi, Masatomo; Asami, Tadao; Nakajima, Masatoshi
• Is Part Of: Bioorganic & medicinal chemistry letters. Volume 28:Issue 14(2018)
• Page Start: 2465
• Page End: 2470
• Publication Date: 2018-08-01
• Subjects: Terpenoid -- GA-like -- Natural product -- GID1 -- Plant hormone -- Selectivity; Bioorganic chemistry -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1016/j.bmcl.2018.06.005
• Languages: English
• ISSNs: 0960-894X

Abstract

Graphical abstract: Highlights: The H-acid analog (5) shows higher hypocotyl elongation activity than H-acid does. The hypocotyl elongation induced by analog (5) depends on binding to AtGID1a. The analog (5) preferentially promotes the formation of the AtGID1a-DELLA complex. Abstract: Helminthosporol, a natural growth regulator isolated from a fungus, stimulates hypocotyl growth and seed germination, similar to gibberellin (GA). We recently reported that helminthosporic acid (H-acid), a synthetic analog of helminthosporol, acts as an agonist of GA receptor. In this study, we showed that a H-acid analog, in which the hydroxymethyl group at the C-8 position of H-acid was converted to a keto group, acts as a selective GA receptor agonist. 1) This analog shows higher hypocotyl elongation activity in Arabidopsis than H-acid does, and induces the degradation of DELLA protein and 2) leads to the formation of the GID1-DELLA complex and 3) regulates the expression of GA-related genes. In addition, 4) its hypocotyl elongation activity was not observed in a atgid1a single mutant, and 5) this analog could promote only the interaction between specific GA receptors and DELLA proteins in vitro . Taken together, our results strongly suggest that the selectivity of the reported H-acid analog depends on the specificity of its GA receptor binding activity.