Comparing Phenotypes of IQG1 Mutants
Department
Biological Sciences
Major
Biological Sciences
Research Advisor
Shannon, Katie
Advisor's Department
Biological Sciences
Funding Source
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 (2A) that has two serines mutated to alanine and a mutant (4A) that has three serines and one threonine mutated to alanine are compared in relation to the wild type strain. Investigation of another mutant (3T) has 3 serines mutated to theronines that is able to be phosphorylated but unable to be dephosphorylated, which is suspected to cause a lethal phenotype. The goal in doing this is to compare cytokinesis defects in the 2A 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 Senior at Missouri University of Science and Technology pursuing a degree in Biological Sciences with an emphasis in pre medicine. She is a member of Scrubs Pre-Med Club, Zeta Tau Alpha, Phi Sigma Biological Honor Society, and has been conducting research in Dr. Shannon’s cytokinesis lab for three years. She plans on pursuing a MD/Ph.D. once she graduates from Missouri S&T.
Research Category
Sciences
Presentation Type
Oral Presentation
Document Type
Presentation
Award
Sciences oral presentation, Third place
Location
Carver Room
Presentation Date
11 Apr 2017, 10:20 am - 10:40 am
Comparing Phenotypes of IQG1 Mutants
Carver 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 (2A) that has two serines mutated to alanine and a mutant (4A) that has three serines and one threonine mutated to alanine are compared in relation to the wild type strain. Investigation of another mutant (3T) has 3 serines mutated to theronines that is able to be phosphorylated but unable to be dephosphorylated, which is suspected to cause a lethal phenotype. The goal in doing this is to compare cytokinesis defects in the 2A 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.
