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Harold Erickson

James B. Duke Professor
Cell Biology
919 684 6385
Research Interest: 
Cell biophysics
Microbiology and virology
Molecular structure
Research Summary: 
Cytoskeleton and cell motility, especially the bacterial tubulin homolog FtsZ, the key player in bacterial cell division; Extracellular matrix, especially fibronectin.
Research Description: 

FtsZ and bacterial cell division. Our most important discovery was the reconstitution of FtsZ rings inside liposomes, achieved by Asst Res Prof Masaki Osawa and published in Science in 2008. This reconstitution showed that the Z ring could be assembled from purified FtsZ, and did not need any of the dozen other cell division proteins found in bacteria. Of equal importance, we demonstrated that these reconstituted Z rings generated a constriction force on the liposomes, again without any other proteins. Subsequent work supported a model that the constriction force is generated by bending protofilaments.

Extracellular matrix: We have used FN-GFP to demonstrate that FN matrix fibrils are very elastic, and are now working to resolve two possible mechanisms. One mechanism postulates that tension causes FNIII domains to unravel. Our evidence suggests that domains to not unravel, and that stretching involves changes of the large FN molecules from a compact pretzel conformation to a more extended form.

Inside-out Z rings--constriction with and without GTP hydrolysis.
Osawa M, Erickson HP.
Mol Microbiol. 2011. 81:571-9.

Reconstitution of contractile FtsZ rings in liposomes.
Osawa M, Anderson DE, Erickson HP.
Science. 2008. 320:792-4.

Evolution of the cytoskeleton.
Erickson HP.
Bioessays. 2007. 29:668-77.