PUBLICATIONS - M. Lou Ernst-Fonberg

M. Lou Ernst-Fonberg, Professor. (ernstfon@etsu.edu) M.D. Temple University School of Medicine, Ph.D. Yale University. Molecular biology and biochemistry E. coli hemolysin toxin activation. A benign protein is made toxic (lyses erythrocytes) by fatty acylation (2 fatty acyl groups) catalyzed by a specific acyltransferase. The biology of the toxin system is used to study molecular mechanisms of protein-protein recognition and cellular signal propagation. 

Worsham, L.M.S., Earls, L., Jolly, C., Gordon, K.G., Trent, M.S., and Ernst-Fonberg, M.L. 2003. Amino acid residues of Escherichia coli acyl carrier protein involved in heterologous protein interactions.  Biochemistry 42, 167-176.

Worsham, L., Trent, M.S., Earls, L, Jolly, C. and Ernst-Fonberg, M.L.  2001.  Insights into the catalytic mechanism of HlyC, the internal protein acyltransferase that activates Escherichia coli hemolysin toxin.  Biochemistry 40, 13607-13616.

Trent, M.S., Worsham,L. and Ernst-Fonberg, M.L. 1999. HlyC, the internal protein acyltransferase that activates hemolysin toxin: Roles of various conserved residues in enzymatic activity as probed by site-directed mutagenesis.  Biochemistry 38, 9541-9548.

Trent, M.S., Worsham,L. and Ernst-Fonberg, M.L. 1999. HlyC, the internal protein acyltransferase that activates hemolysin toxin:  the role of conserved tyrosin and arginine residues in enzymatic activity as probed by chemical modification and site-directed mutagenesis.  Biochemistry, 38, 8831-8838.

Trent, M.S., Worsham, L., and Ernst-Fonberg, M.L. 1999. HlyC, the internal protein acyltransferase that activates hemolysin toxin: role of conserved histidine, serine and cysteine residues in enzymatic activity as probed by chemical modification and site-directed mutagenesis.  Biochemistry 38, 3433-3439.

Trent, M.S., Worsham, L., and Ernst-Fonberg, M.L. 1998.  The biochemistry of hemolysin toxin activation: characterization of HlyC, an internal protein acyltransferase. Biochemistry 37: 4644-4652.