Title

Phenotype Comparison of two Different IQG1 Mutant Alleles

Presenter Information

Madison Mara

Department

Biological Sciences

Major

Biological Sciences

Research Advisor

Shannon, Katie

Advisor's Department

Biological Sciences

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 two 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. The goal in doing this is to compare cytokinesis defects in the 3A mutant and the 4A mutant and see if threonine has a unique function. To confirm mutant phenotype, morphological analysis will be performed via microscopy and immunofluorescence to indicate if actin ring formation has been disrupted.

Biography

Madison Mara is a freshman majoring in biological sciences and plans to enter medical school at the end of her undergrad. She has been working in Dr.Shannon’s cytokinesis lab since June 2014 and this represents her first project. She is currently the Community Chair on the Executive Committee for Scrubs and a member of Helix.

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

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Apr 15th, 9:00 AM Apr 15th, 11:45 AM

Phenotype Comparison of two Different IQG1 Mutant Alleles

Upper Atrium/Hall

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 two 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. The goal in doing this is to compare cytokinesis defects in the 3A mutant and the 4A mutant and see if threonine has a unique function. To confirm mutant phenotype, morphological analysis will be performed via microscopy and immunofluorescence to indicate if actin ring formation has been disrupted.