Dragwidge Jonathan

Dragwidge Jonathan - Postdoctoral fellow
Joined the group in 2019

Jonathan Dragwidge obtained his PhD in 2017 in La Trobe University, Australia where he studied the role of sodium hydrogen exchangers in plant development and trafficking under supervision of Tony Gendall. After finishing his PhD he joined the lab of Karin Schumacher at the Centre for Organismal Studies (COS) in Heidelberg, Germany. Here he used live-cell imaging approaches to study the dynamics of the Golgi complex and trans-Golgi network (TGN). In 2019, he joined the lab of Daniel Van Damme to investigate the role of the TPLATE complex in clathrin-mediated endocytosis. His work demonstrate that the TPLATE complex assembles into liquid-like compartments known as biomolecular condensates, and that this process catalyses the assembly of clathrin-coated vesicles. He is currently funded by an FWO postdoctoral fellowship since 2021.

Microscopy Imaging tools at PSB

Microscopy Imaging tools at PSB

 

PSB researchers are actively involved in generating tools to allow real-time visualization of plants under conditions that disturb specific processes. Examples are the use of microfluidics setups to monitor the effect of chemical compounds as well as the effect of altered temperature, on cellular dynamics. 

Temperature-modulated live cell imaging

Temperature-modulated live cell imaging.

Dynamic imaging of fast-occurring processes is hampered by the fact that the signal/noise ratio of a fluorescent image is inversely related to the exposure time. The exposure time in turn limits the imaging speed and thereby the temporal resolution. We are increasing the temporal resolution of live-cell imaging plant samples by modulating the temperature of the samples in situ on the microscope stage as lowering the temperature slows down biological processes.

Developing proximity biotinylation assays in plants to expand the interactomics toolbox

Developing proximity biotinylation assays in plants to expand the interactomics toolbox.

Proximity biotinylation uses a promiscuous biotin ligase, which causes biotinylation of proteins in the vicinity of the bait. These biotinylated proteins can be identified using mass spectrometry without the need to maintain the protein-protein interactions during the purification. This tool is therefore especially suited for interactions between cytosolic and transmembrane proteins. We are designing protocols to adequately perform proximity biotinylation in plants.

Visualizing protein-protein interactions in plants

Visualizing protein-protein interactions in plants

To gain insight into protein-protein interactions that occur in planta, we expanded the interaction assay toolkit. We have developed Knocksideways in plants (KSP) as an imaging-based protein-protein interaction assays to visualize binary as well as higher-order interactions by. KSP can be compared to an intracellular Co-IP experiment. The tool uses the ability of rapamycin to alter the localization of a bait protein and its interactors via the heterodimerization of FKBP and FRB domains.

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