The Interaction of Mid1 and F-actin During Cytokinesis in Fission Yeast
Location
Exhibition Hall, DeVos Center
Description
Mid1 is a protein in the fission yeast Schizzosaccharomyces pombe that is important for proper cell division. Before cytokinesis, Mid1 anchors to the plasma membrane providing a scaffold for actin binding and bundling proteins leading to the central positioning of the actin-myosin contractile ring. The placement of the ring dictates the position of constriction and ultimate division of the cell into two genetically identical daughter cells. Deletion of the mid1 gene causes misplacement of the contractile ring resulting in uneven segregation of the genetic material during cytokinesis. F-actin is the major component of the contractile ring and preliminary results indicate the C-terminus of purified Mid1 binds this cytoskeletal element. To further clarify the Mid1 actin-binding domain, five GST-fusion proteins spanning the Mid1 C-terminus were produced and purified. The fragments were individually analyzed for association with actin filaments by cosedimentation assay. Future experiments will focus on the roles of the Mid1 binding domain to F-actin in actin polymerization, localization, and stability during contractile ring formation. Clarification of the interaction of Mid1 with F-actin may reveal an important regulatory step for proper cytokinesis and can help explain the vast regulatory roles of Mid1 during contractile ring formation in fission yeast.
The Interaction of Mid1 and F-actin During Cytokinesis in Fission Yeast
Exhibition Hall, DeVos Center
Mid1 is a protein in the fission yeast Schizzosaccharomyces pombe that is important for proper cell division. Before cytokinesis, Mid1 anchors to the plasma membrane providing a scaffold for actin binding and bundling proteins leading to the central positioning of the actin-myosin contractile ring. The placement of the ring dictates the position of constriction and ultimate division of the cell into two genetically identical daughter cells. Deletion of the mid1 gene causes misplacement of the contractile ring resulting in uneven segregation of the genetic material during cytokinesis. F-actin is the major component of the contractile ring and preliminary results indicate the C-terminus of purified Mid1 binds this cytoskeletal element. To further clarify the Mid1 actin-binding domain, five GST-fusion proteins spanning the Mid1 C-terminus were produced and purified. The fragments were individually analyzed for association with actin filaments by cosedimentation assay. Future experiments will focus on the roles of the Mid1 binding domain to F-actin in actin polymerization, localization, and stability during contractile ring formation. Clarification of the interaction of Mid1 with F-actin may reveal an important regulatory step for proper cytokinesis and can help explain the vast regulatory roles of Mid1 during contractile ring formation in fission yeast.