Protein-protein interactions as they appear in functional protein complexes have been studied in high throughput fashion in yeast via the in vivo expression of ‘tagged’ proteins and the subsequent retrieval of proteins bound to this ‘bait’. Especially the tandem affinity purification (TAP) method elegantly demonstrates the strength of such protein complex studies. We have developed a unique TAP technology platform for complex isolation from plant cells.
Complex purifications are performed on cell suspension cultures or whole seedlings. Co-purified proteins are identified by mass-spectrometry in close collaboration with the Centre for Proteomics and Mass Spectrometry at Antwerp University. Recently, we were able to build a cell cycle interactome around 100 cell cycle proteins, delivering more than 100 new candidate cell cycle proteins and offering a comprehensive view on the core cell cycle complex machinery. We will continue to broaden our complex purification technology towards the isolation of protein complexes from plant organs such as leaf and root, and from crop species such as corn, towards the isolation of complexes containing membrane proteins, and towards the isolation of transient interactions.