The opportunistic pathogen Pseudomonas aeruginosa uses quorum sensing to communicate among bacteria cells and regulate gene expression. One of the intercellular signaling molecules that is involved in quorum sensing is Pseudomonas quinolone signal (PQS), which has multiple functions including influencing the virulence of the pathogen. The regulatory protein PqsR is involved in the PQS system, binds to PQS, and intriguingly associates with the plasma membrane despite predictions based on its sequence that it is a soluble protein. Because of this membrane association, PqsR is thought to receive PQS by interacting with a membrane protein that transports PQS through the cell membrane. Pulldown assays followed by mass spectrometry identified a protein that potentially associates with PqsR. A series of pulldown and reciprocal pulldown experiments were carried out in order to validate the protein-protein interaction. Different protein tags were attached onto the proteins and used for their detection by Western blotting; however, these experiments did not provide enough evidence for the interaction due to protein expression and solubility issues. Further work needs to be carried out to confirm the validity of this putative interacting partner of PqsR. While conducting this research this summer, I was also fortunate enough to be able to experience the diversity of attractions, foods, and cultures within Singapore as well as throughout Southeast Asia.<br/>

Undergraduate research in Singapore: Explorations of protein-protein interactions and Southeast Asia

253rd National Meeting (2017)

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