HAROLD ERICKSON
James B. Duke Professor,
Department of Cell Biology

Contact Information
367 Nanaline Duke, Box 3709 Med Ctr
(PH) 919-684-6385
(FX) 919-684-8090
h.erickson@cellbio.duke.edu

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Education

	PhD	Development and analysis of proposed techniques for nucleic acid sequence study by electron microscopy, Biophysics, The Johns Hopkins University, 1968
	BS	Physics, Carnegie-Mellon University, 1962

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Experience

	1988- present	Professor of Cell Biology, Department of Cell Biology, Duke University Medical Center, Durham, NC.
	1988-1990	Interim Chairman, Department of Cell Biology, Duke University Medical Center, Durham, NC.
	1970-1988	Assistant Professor and Professor, Department of Anatomy, Duke University Medical Center, Durham, NC.
	1968-1970	Postdoctoral Research Trainee, MRC Laboratory of Molecular Biology, Cambridge, England. Training under A. Klug in optical and computer image processing in electron microscopy.

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Selected Publications

1. Stricker, J., P. Maddox, E.D. Salmon, and H.P. Erickson. 2002. Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching. PNAS. 99:3171-2659.
2. Romberg, L., M. Simon, and H.P. Erickson. 2001. Polymerization of FtsZ, a bacterial homolog of tubulin: Is assembly cooperative? J. Biol. Chem. 276:11743-11753.
3. Lu, C.L., M. Reedy, and H.P. Erickson. 2000. Straight and curved conformations of FtsZ are regulated by GTP hydrolysis. J. Bacteriol. 182:164-170.
4. Redick, S.D., D.L. Settles, G. Briscoe, and H.P. Erickson. 2000. Defining fibronectin's cell adhesion synergy site by site-directed mutagenesis. J. Cell Biol. 149:521-527.
5. Ohashi, T., D.P. Kiehart, and H.P. Erickson. 2002. Dual labeling of the fibronectin matrix and actin cytoskeleton with green fluorescent protein variants. J. Cell Sci. 115:1221-9.

 

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Synergistic Activities

• Rotary shadowing EM. Dr. Erickson maintains a facility at Duke to determine the structure of single protein molecules by rotary shadowing electron microscopy. He seeks applications from Duke, other labs around the country, and internationally.
• Erickson web page. Dr. Erickson maintains a web page that makes publicly available notes on protein structure and association, an updated table of bacterial cell division genes, and miscellaneous data and analysis tools.

 

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Collaborators

Julio Fernandez (Mayo); Piotr Marszalek (Duke); Chenquang Lu (Duke); Daniel Kiehart (Duke); Tomoo Ohashi (Duke)

Ph.D. Advisor: Michael Beer, The Johns Hopkins University

Postdoctoral Advisor: Aaron Klug, MRC Laboratory of Molecular Biology (UK)

Research Support:

• Dr. Erickson is a PI on 3 active grants: NIH 066014-01, NIH CA47056-22; ONR Free Electron Laser grant program.
• Dr. Erickson is an investigator on NIH CA14236-27;
  

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Research Interest

Cytoskeleton and cell motility, with current focus on bacterial cell division; extracellular matrix, with current focus on fibronectin; protein structure and self assembly.

Cytoskeleton: It is now clear that the cytoskeleton originated in bacteria. The bacterial actin is MreB, and the bacterial tubulin is FtsZ. Our major research is on FtsZ, which assembles into a contractile ring that divides the bacterium. Unfortunately, the structure of the Z-ring has never been imaged by EM. We have studied the in vitro assembly of FtsZ by electron microscopy, and have discovered two polymer forms that likely form the basis for the Z-ring in vivo. FtsZ assembles into thin protofilaments that can switch from a straight conformation in GTP to a sharply curved ring in GDP. We believe that this conformational change may provide the force for contraction – i.e., FtsZ may be the motor as well as the cytoskeletal framework.

Our long term goals are two-fold. First, to understand the mechanism of bacterial cell division (which is surprisingly less well understood than division of eukaryotic cells). Second, to learn basic principles of assembly that will apply to both FtsZ and tubulin. Many experiments that are impossible with tubulin can be done easily with FtsZ. Although our current work is with FtsZ, we hope to develop parallel studies of MreB, the bacterial actin.

Extracellular Matrix: A second interest of our lab is extracellular matrix and cell adhesion, focusing now on fibronectin. We have discovered that the FN matrix is very elastic, and are studying the mechanism of the elasticity. We are also interested in the mechanics of the fibronectin-integrin bond, and how much force can it sustain relative to that needed to stretch the fibrils. We have recently obtained a conditional fibronectin knockout in mice, using the cre/lox system, which will let us investigate the role of FN in later development and in the adult (the complete knockout is embryonic lethal).

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