James B Duke Professor, Department of Cell Biology, Duke University Medical Center
Our laboratory is interested in the structural biochemistry of two systems the cytoskeleton and the extracellular matrix. Our work on cytoskeleton is now focused on FtsZ, the major bacterial cytoskeletal protein that powers division in all bacteria. FtsZ is a homolog of tubulin, so what we learn has implications for the eukaryotic cytoskeleton. We are trying to determine how FtsZ assembles into the contractile ring and generates the force to divide bacteria. We are using in vitro assembly studies and site directed mutagenesis. Recently we have developed fluorescence techniques, which demonstrate extremely fast assembly dynamics in vitro and in vivo. We are now working to develop single molecule (TIRF) fluorescence microscopy to follow the assembly dynamics of single FtsZ protofilaments. Our ultimate goal is to be able to recreate a contractile band based on FtsZ.
Our work on the extracellular matrix focuses primarily on fibronectin. We have made a GFP-fibronectin construct that permits us to follow the assembly of the fibronectin matrix in real time. We have found that the matrix fibrils are highly elastic, and are now seeking the mechanism for stretching. Again, fluorescence techniques are proving powerful tools to probe stretching at the molecular level.
In the role of Faculty Member, Harold Erickson contributes recommendations and reviews to the Macromolecular Assemblies & Machines Section in the Structural Biology Faculty, writing brief accessible comments to summarize the value of the articles and adding rating score.
The Faculty comprises Heads of Faculty, Heads of Section, Faculty Members and Associate Faculty Members, as well as an International Advisory Board.
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