Comparing Phenotypes of IQG1 Mutants
Department
Biological Sciences
Major
Biological Sciences
Research Advisor
Shannon, Katie
Advisor's Department
Biological Sciences
Funding Source
Opportunities for Undergraduate Research Experiences (OURE)
Abstract
During cytokinesis, many mutations can arise that affect formation of the actomyosin ring. Iqg1 is a protein that is required for assembly and contraction of the actomyosin ring in budding yeast. This project is designed to compare the phenotypes of three separate IQG1 mutant alleles to examine any problems that arise during cytokinesis. In this research, a mutant (3A) that has three serines dephosphorylated via CDC14 mutated to alanine is compared to a mutant (4A) that has three serines and one threonine mutated to alanine and a mutant (3T) that has 3 serines mutated to theronines. This 3T mutant is able to be phosphorylated but it unable to be dephosphorylated. The goal in doing this is to compare cytokinesis defects in the 3A mutant, 4A mutant, and 3T mutant and see if threonine has a unique function and determine the phenotype of permanent phosphorylation. To confirm mutant phenotype, morphological analysis will be performed via microscopy and immunofluorescence to indicate if actin ring formation has been disrupted.
Biography
Madison is a Junior at Missouri University of Science and Technology pursuing a degree in Biological Sciences with an emphasis in pre medicine. She is the Vice President of Scrubs Pre-Med Club, the Director of Philanthropy for Zeta Tau Alpha, and has been conducting research in Dr. Shannon’s cytokinesis lab for two years. She plans on going to medical school once she graduates from Missouri S&T.
Research Category
Sciences
Presentation Type
Oral Presentation
Document Type
Presentation
Award
Sciences oral presentation, First place
Location
Ozark Room
Presentation Date
11 Apr 2016, 10:00 am - 10:30 am
Comparing Phenotypes of IQG1 Mutants
Ozark Room
During cytokinesis, many mutations can arise that affect formation of the actomyosin ring. Iqg1 is a protein that is required for assembly and contraction of the actomyosin ring in budding yeast. This project is designed to compare the phenotypes of three separate IQG1 mutant alleles to examine any problems that arise during cytokinesis. In this research, a mutant (3A) that has three serines dephosphorylated via CDC14 mutated to alanine is compared to a mutant (4A) that has three serines and one threonine mutated to alanine and a mutant (3T) that has 3 serines mutated to theronines. This 3T mutant is able to be phosphorylated but it unable to be dephosphorylated. The goal in doing this is to compare cytokinesis defects in the 3A mutant, 4A mutant, and 3T mutant and see if threonine has a unique function and determine the phenotype of permanent phosphorylation. To confirm mutant phenotype, morphological analysis will be performed via microscopy and immunofluorescence to indicate if actin ring formation has been disrupted.
