Biology subjects

Yoo, N.

Publications and source records attributed to Yoo, N..

4 recordsLinked to original sources

bioRxiv2026

Hopeaphenol targets histidine kinase signaling across kingdoms to suppress bacterial virulence and potentiate plant immunity

Small molecules can control plant disease either by disarming the pathogen or by priming host immunity, but single compounds that do both are rare and mechanistically unexplained. Here we show that hopeaphenol (HP), a resveratrol tetramer from stilbene producing plants, acts on histidine kinase (HK) signaling on both sides of the Arabidopsis-Pseudomonas interaction. In Pseudomonas syringae pv. tomato DC3000, HP represses the type III secretion regulon and motility genes, restricts surface motility independently of effector delivery, and binds a defined subset of virulence-associated sensor kinases while reducing their autophosphorylation; comparable engagement occurs in Pectobacterium atrosepticum. Binding and inhibition depend on the tetrameric scaffold rather than the resveratrol monomer. In the host, HP binds the CHASE domains of the cytokinin receptors AHK2, AHK3 and AHK4 and elicits an immune-associated, rather than canonical cytokinin, transcriptional output. HP-dependent potentiation of PTI and ETI responses and early restriction of bacterial growth require AHK3 and AHK4. HP thus coordinates opposing outputs from divergent HK systems across kingdoms.

plant biology↗

bioRxiv2023

A natural cyclic peptide valinomycin enhances plant innate immunity

Various natural compounds as alternative agents for the chemical management of plant diseases have long been proposed. Valinomycin, a Streptomyces-derived cyclic peptide, acts as an antifungal agent against several plant pathogenic fungi, including Botrytis cinerea. Here, we report the novel function of valinomycin, plant immune-boosting. Valinomycin potentiates pattern-triggered immunity (PTI) and effector-triggered immunity (ETI) in Arabidopsis, leading to enhanced resistance against bacterial speck disease locally and systemically. Moreover, this plant immune-boosting activity of valinomycin is associated with plant hormonal signaling. Thus, we propose that valinomycin harbors potential as a biocontrol agent suppressing complex pathogen infections, such as bacteria and fungi.

plant biology↗

bioRxiv2019

The engulfment receptor Draper organizes the postsynaptic spectrin cytoskeleton into corrals containing synaptic proteins and promotes synaptic renewal

The spectrin cytoskeleton is required for development of the Drosophila neuromuscular junction (NMJ) but its role is unclear. Here we show that the muscle spectrin lattice functions to corral membrane-associated synaptic proteins and limit their lateral mobility. Drosophila adducin, Hts, is required for integrity of the spectrin cytoskeleton and disruption of Hts function results in failure of the corrals. The spectrin cytoskeleton is itself patterned at the muscle membrane by the engulfment receptor Draper (Drpr) through regulation of Hts. We find patches of membrane where the spectrin cytoskeleton is organized into bilaterally symmetric patterns, which coincide with a field of Drpr-dependent structures similar to phagocytic pseudopods. The bilaterally symmetric patterns are likely created by folds of the muscle membrane in the pseudopods. We present evidence that the folds trap nascent boutons of motor neurons, leading to boutons with a bilaterally symmetric organization of the postsynaptic membrane. Drpr thus acts as a sensor of synaptic damage that promotes synaptogenesis.

developmental biology↗

bioRxiv2019

Mechanistic Insights into the Protective Roles of Polyphosphate Against Amyloid Cytotoxicity

The universally abundant polyphosphate (polyP) accelerates fibril formation of disease-related amyloids and protects against amyloid cytotoxicity. To gain insights into the mechanism(s) by which polyP exerts these effects, we focused on -synuclein, a well-studied amyloid protein, which constitutes the major component of Lewy bodies found in Parkinsons Disease. Here we demonstrate that polyP is unable to accelerate the rate-limiting step of -synuclein fibril formation but effectively nucleates fibril assembly once -synuclein oligomers are formed. Binding of polyP to -synuclein either during fibril formation or upon fibril maturation substantially alters fibril morphology, and effectively reduces the ability of -synuclein fibrils to interact with cell membranes. The effect of polyP appears to be -synuclein fibril specific, and successfully prevents the uptake of fibrils into neuronal cells. These results suggest that altering the polyP levels in the extracellular space might be a potential therapeutic strategy to prevent the spreading of the disease.

cell biology↗