Event Title

Association of Anillin-Like Protein Mid1 with Actin

Location

Steelcase Lecture Hall

Start Date

31-3-2011 4:30 PM

Description

The scaffolding protein Mid1 (middle 1), found in the fission yeast Schizosaccharomyces pombe, is thought to function as a scaffolding protein. This anillin-like protein assists in the assembly and placement of the actin contractile ring by directly associating with the cell cortex and components of the contractile ring to anchor the structure in the cell center. The placement and functionality of the division septum corresponds to the placement of the contractile ring. Therefore, identifying contractile ring proteins that directly associate with Mid1 will contribute to our understanding of proper cell division and equal transfer of the cellular contents, including the genetic material. Our preliminary results suggest that Mid1 contributes to the formation and placement of the actin contractile ring through the direct association of F-Actin filaments. The main goals of this research project are to identify the actin binding domain in Mid1 and analyze the phenotypic consequence of disrupting the interaction. To test this, we are using actin cosedimentation assays with purified regions of Mid1 protein. After identifying the actin binding region within Mid1, Mid1 mutants with alterations to the actin binding region will be generated and analyzed for cell division defects.

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Mar 31st, 4:30 PM

Association of Anillin-Like Protein Mid1 with Actin

Steelcase Lecture Hall

The scaffolding protein Mid1 (middle 1), found in the fission yeast Schizosaccharomyces pombe, is thought to function as a scaffolding protein. This anillin-like protein assists in the assembly and placement of the actin contractile ring by directly associating with the cell cortex and components of the contractile ring to anchor the structure in the cell center. The placement and functionality of the division septum corresponds to the placement of the contractile ring. Therefore, identifying contractile ring proteins that directly associate with Mid1 will contribute to our understanding of proper cell division and equal transfer of the cellular contents, including the genetic material. Our preliminary results suggest that Mid1 contributes to the formation and placement of the actin contractile ring through the direct association of F-Actin filaments. The main goals of this research project are to identify the actin binding domain in Mid1 and analyze the phenotypic consequence of disrupting the interaction. To test this, we are using actin cosedimentation assays with purified regions of Mid1 protein. After identifying the actin binding region within Mid1, Mid1 mutants with alterations to the actin binding region will be generated and analyzed for cell division defects.