Determining which Domain of Iqg1 Binds to Formins during Cytokinesis
Department
Biological Sciences
Major
Biological Sciences
Research Advisor
Shannon, Katie
Advisor's Department
Biological Sciences
Funding Source
Opportunities for Undergraduate Research (OURE)
Abstract
The final step in cell division is cytokinesis. Cytokinesis must be coordinated with mitosis in order to prevent aneuploidy. Budding yeast are a good model organism for studying cytokinesis due to genetic and molecular tools and inexpensive growth medium. Iqg1 is a protein that has been shown to regulate cytokinesis in budding yeast cells. The Iqg1 protein contains four domains: IQ motifs that are needed for localization of Iqg1 to the contractile ring, a CHD domain required for actin recruitment, a GAP domain essential for contraction, and a RGCT domain that was predicted to interact with formins Bni1 and Bnr1. However, we found that a deletion of the RGCT domain of the protein is still able to interact with the formins and is required for cell viability. Our current goal is to determine domain of the protein that is responsible for formin binding using different mutant strains.
Biography
Brandon Drennen is from the small town of Freeburg in Missouri. He has been attending the Missouri University of Science and Technology for 4 years now and will graduate this May. After graduation he will be moving to Baltimore, MD to attend grad school and work on his PhD in Pharmaceutical Sciences.
Research Category
Sciences
Presentation Type
Poster Presentation
Document Type
Poster
Location
Upper Atrium/Hall
Presentation Date
16 Apr 2014, 9:00 am - 11:45 am
Determining which Domain of Iqg1 Binds to Formins during Cytokinesis
Upper Atrium/Hall
The final step in cell division is cytokinesis. Cytokinesis must be coordinated with mitosis in order to prevent aneuploidy. Budding yeast are a good model organism for studying cytokinesis due to genetic and molecular tools and inexpensive growth medium. Iqg1 is a protein that has been shown to regulate cytokinesis in budding yeast cells. The Iqg1 protein contains four domains: IQ motifs that are needed for localization of Iqg1 to the contractile ring, a CHD domain required for actin recruitment, a GAP domain essential for contraction, and a RGCT domain that was predicted to interact with formins Bni1 and Bnr1. However, we found that a deletion of the RGCT domain of the protein is still able to interact with the formins and is required for cell viability. Our current goal is to determine domain of the protein that is responsible for formin binding using different mutant strains.
