Dual Role of Strigolactone Receptor Signaling Partner in Inhibiting Substrate Hydrolysis
journal contributionposted on 2022-03-11, 20:03 authored by Briana L. Sobecks, Jiming Chen, Diwakar Shukla
Plant branch and root growth relies on metabolism of the strigolactone (SL) hormone. The interaction between the SL molecule, Oryza sativa DWARF14 (D14) SL receptor, and D3 F-box protein has been shown to play a critical role in SL perception. Previously, it was believed that D3 only interacts with the closed form of D14 to induce downstream signaling, but recent experiments indicate that D3, as well as its C-terminal helix (CTH), can interact with the open form as well to inhibit strigolactone signaling. Two hypotheses for the CTH induced inhibition are that either the CTH affects the conformational ensemble of D14 by stabilizing catalytically inactive states or the CTH interacts with SLs in a way that prevents them from entering the binding pocket. In this study, we have performed molecular dynamics (MD) simulations to assess the validity of these hypotheses. We used an apo system with only D14 and the CTH to test the active site conformational stability and a holo system with D14, the CTH, and an SL molecule to test the interaction between the SL and CTH. Our simulations show that the CTH affects both active site conformation and the ability of SLs to move into the binding pocket. In the apo system, the CTH allosterically stabilized catalytic residues into their inactive conformation. In the holo system, significant interactions between SLs and the CTH hindered the ability of SLs to enter the D14 binding pocket. These two mechanisms account for the observed decrease in SL binding to D14 and subsequent ligand hydrolysis in the presence of the CTH.
Read the peer-reviewed publication
subsequent ligand hydrolysisroot growth reliesrecent experiments indicateperformed molecular dynamicsinduce downstream signalingtwo mechanisms accountactive site conformationoryza sativa </inhibit strigolactone signalingcth induced inhibitiond14 binding pocketbinding pocketinactive conformationholo </apo </sl bindingtwo hypothesesterminal helixsignificant interactionsopen formobserved decreasedual rolecth hinderedcth affectscth ),critical roleconformational ensembleclosed formbox protein