Spire works with Cappuccino to build actin filaments in the cell. Both proteins play an important role in polarity establishment in Drosophila oocytes by constructing the actin meshwork. Myosin V is a motor protein that travels along actin filaments like those that Spire and Cappuccino construct. Previous research suggests that Myosin V and Spire interact. We hypothesize that Myosin V is activated by Spire, but that the binding of Myosin V and Spire has no effect on Spire’s activity. In order to test this, we purified the two proteins from E. coli and tested their binding in a pulldown assay. The purpose of this study is to measure binding of Myosin V and Spire and learn how it affects each of their functions. In order to test for binding of Spire and Myosin V, we performed a pulldown assay with wildtype and mutated Spire and Myosin V. Results suggest when either Spire or Myosin V are mutated, binding is greatly reduced compared to binding of wildtype Spire and wildtype Myosin V. This shows that mutating either Spire or Myosin V affects binding of the two proteins. Analysis of Spire’s actin assembly in vitro coupled with in vivo data using the Drosophila oocyte as a system will reveal the importance of the Spire-Myosin V interaction. We predict that the disruption of binding between Spire and Myosin V will negatively affect viability and meshwork formation in Drosophila oocytes.

Investigating the binding of spire/myosin-V in drosophila melanogaster

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.