Colocalization effects of Pch and ParP on chemotaxis proteins in Pseudomonas aeruginosa
Mentor 1
Sonia Bardy
Location
Union Wisconsin Room
Start Date
29-4-2016 1:30 PM
End Date
29-4-2016 3:30 PM
Description
Pseudomonas aeruginosa is a gram negative, rod shaped, opportunistic pathogen that is known for infecting the lungs of cystic fibrosis patients as well as burn victims. P. aeruginosa has a single flagellum located at the pole of the cell and uses chemotaxis proteins to control the flagellum which ultimately directs swimming towards or away from a stimulus. These chemotaxis proteins are localized to the pole using partitioning proteins ParP and ParC. Improper inheritance of these partitioning proteins leads to a lack of chemotaxis foci and a reduction of swimming motility. We hypothesized that Pch, a phosphodiesterase responsible for regulating c-di-GMP levels in P. aeruginosa, may interact with ParP and play a role in its function. To test our hypothesis, we assayed protein interactions between Pch and ParP using the bacterial two hybrid assay. In addition, constructs were made containing pch and parP along with fluorescence tags and protein localization was analyzed using fluorescence microscopy. The results of our bacterial two hybrid assay show that there is in fact an interaction between Pch and ParP. Because of the fact that there is an interaction between Pch and ParP we propose that Pch has some effect on the function of ParP. Further work with fluorescence microscopy will be conducted to test to localization of both Pch and ParP and to see what exact role they place with each other.
Colocalization effects of Pch and ParP on chemotaxis proteins in Pseudomonas aeruginosa
Union Wisconsin Room
Pseudomonas aeruginosa is a gram negative, rod shaped, opportunistic pathogen that is known for infecting the lungs of cystic fibrosis patients as well as burn victims. P. aeruginosa has a single flagellum located at the pole of the cell and uses chemotaxis proteins to control the flagellum which ultimately directs swimming towards or away from a stimulus. These chemotaxis proteins are localized to the pole using partitioning proteins ParP and ParC. Improper inheritance of these partitioning proteins leads to a lack of chemotaxis foci and a reduction of swimming motility. We hypothesized that Pch, a phosphodiesterase responsible for regulating c-di-GMP levels in P. aeruginosa, may interact with ParP and play a role in its function. To test our hypothesis, we assayed protein interactions between Pch and ParP using the bacterial two hybrid assay. In addition, constructs were made containing pch and parP along with fluorescence tags and protein localization was analyzed using fluorescence microscopy. The results of our bacterial two hybrid assay show that there is in fact an interaction between Pch and ParP. Because of the fact that there is an interaction between Pch and ParP we propose that Pch has some effect on the function of ParP. Further work with fluorescence microscopy will be conducted to test to localization of both Pch and ParP and to see what exact role they place with each other.
