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Biology subjects

Choi, E. H.

Publications and source records attributed to Choi, E. H..

2 recordsLinked to original sources

Powdery mildew exploits host plastoglobuli functions via DGAT3 and FBN2 for proliferation

Plastoglobuli (PG) are specialized lipid-containing compartments attached to thylakoid membranes within chloroplasts. PGs participate in various metabolic pathways in response to environmental stresses such as high light, nitrogen deficiency, and heat stress. However, their roles in biotic stress remain largely unexplored. In this study, two distinct lines of investigation converge on the importance of PGs to the powdery mildew-Arabidopsis interaction. First, powdery mildew infection results in the accumulation of PGs and PG-localized Arabidopsis Diacylglycerol Acyltransferase 3 (DGAT3), a triacylglycerol biosynthetic enzyme that supports powdery mildew proliferation. Second, a bioinformatic analysis led to the identification of a powdery mildew effector that is PG-localized and interacts specifically with FIBRILLIN 2 (FBN2), one of the most abundant PG core proteins. While silencing the effector limits powdery mildew proliferation, an FBN2 knockout results in increased spore production, providing a direct link between PG function and pathogen manipulation of the host. These findings underscore the significance of PGs in host-pathogen interactions and offer new insights into the intricate mechanisms underlying the interaction of an obligate biotroph with its host. SIGNIFICANCEPlastoglobuli (PG) functions are largely unexplored in the context of host-pathogen interactions. Using the Arabidopsis-powdery mildew system, we uncover new roles for PGs in host-pathogen dynamics through integrated genetic, biochemical, and microscopic analyses. Mutants in PG-localized proteins impact powdery mildew proliferation. Moreover, a powdery mildew effector that interacts with the core PG protein FBN2 is identified and found to contribute to virulence. These findings suggest this obligate biotrophic pathogen exploits PGs for its own gain.

plant biology↗

Dissecting lipid contents in the distinct regions of native retinal rod disk membranes

Photoreceptors rely on distinct membrane compartments to support their specialized function. Unlike protein localization, identification of critical differences in membrane content has not yet been expanded to lipids, due to the difficulty of isolating domain-specific samples. We have overcome this by using SMA to co-immunopurify membrane proteins and their native lipids from two regions of photoreceptor ROS disks. Each samples copurified lipids were subjected to untargeted lipidomic and fatty acid analysis. Extensive differences between center (rhodopsin) and rim (ABCA4 and PRPH2/ROM1) samples included a lower PC to PE ratio and increased LC- and VLC-PUFAs in the center relative to the rim region, which were enriched in shorter, saturated FAs. The comparatively few differences between the two rim samples likely reflect specific protein-lipid interactions. High-resolution profiling of the ROS disk lipid composition provides a model for future studies of other complex cellular structures, and gives new insights into how intricate membrane structure and protein activity are balanced within the ROS. SUMMARYSander et al. have parsed the lipid composition of native-source photoreceptor disks and find large differences in fatty acid unsaturation and chain length between the center and rim regions. They selectively copurify membrane proteins and lipids from each region in SMALPs using nanobodies and antibodies.

cell biology↗