Determining the Function of the RGCt Domain of IQG1 in Budding Yeast
Department
Biological Sciences
Major
Biological Sciences
Research Advisor
Shannon, Katie
Advisor's Department
Biological Sciences
Funding Source
OURE
Abstract
Cytokinesis is the final step in cell division, when the mother cell divides into two daughter cells. In budding yeast, IQG1 is a scaffolding protein that is required for formation and contraction of the actin ring during cytokinesis. The Ras GAP C-terminus domain (RGCt) is one of the four domains found in IQG1. This domain is highly conserved in IQGAP family members, but its function in budding yeast is currently unknown. Based on data from the human homolog, we suspected that this domain would be required for binding to actin-nucleating proteins called formins; however, preliminary data shows that this is not the case. Deletion of the RGCt domain is lethal to yeast cells, so its function is essential. Identifying binding partners for this domain will help determine its function. To do this, we planned to purify a His-tagged RGCt protein from bacteria, incubate with yeast extracts, and identify candidate interacting proteins by western blotting and novel interactions using mass spectrometry.
Biography
Kelsey Crossen is a senior majoring in Biological Sciences with minors in Chemistry and Psychology. She has been an undergraduate researcher in Dr. Katie Shannon’s Cytokinesis Lab since February 2013. Kelsey is heavily involved in S&T’s International Genetically Engineered Machine (iGEM) Team: she was the 2014 secretary and is currently a lab instructor for iGEM’s Lab Training Program. She is also a member of Phi Sigma Biological Sciences Honors Fraternity and and works for the Bio Sci department as a grader. Kelsey also conducted research during summer 2014 at Washington University in St. Louis through the Amgen Scholars program. She will be graduating from S&T this May and plans to enter graduate school in the fall for a doctorate in microbiology.
Research Category
Sciences
Presentation Type
Poster Presentation
Document Type
Poster
Location
Upper Atrium/Hall
Presentation Date
15 Apr 2015, 9:00 am - 11:45 am
Determining the Function of the RGCt Domain of IQG1 in Budding Yeast
Upper Atrium/Hall
Cytokinesis is the final step in cell division, when the mother cell divides into two daughter cells. In budding yeast, IQG1 is a scaffolding protein that is required for formation and contraction of the actin ring during cytokinesis. The Ras GAP C-terminus domain (RGCt) is one of the four domains found in IQG1. This domain is highly conserved in IQGAP family members, but its function in budding yeast is currently unknown. Based on data from the human homolog, we suspected that this domain would be required for binding to actin-nucleating proteins called formins; however, preliminary data shows that this is not the case. Deletion of the RGCt domain is lethal to yeast cells, so its function is essential. Identifying binding partners for this domain will help determine its function. To do this, we planned to purify a His-tagged RGCt protein from bacteria, incubate with yeast extracts, and identify candidate interacting proteins by western blotting and novel interactions using mass spectrometry.
