Phizicky Lab
Jane E. Jackman
Department of Biochemistry and Biophysics, Box 712
(716) 275-1897
University of Rochester School of Medicine and Dentistry
Rochester, NY 14642
Education
| 9/94 - 7/99 | Duke University, Durham, NC. Ph.D. in Biochemistry, 7/99 |
| 9/91 - 5/94 | University of Rochester, Rochester, NY. B.S. in Biochemistry, with Distinction in Research, 5/94 |
| 9/90 - 5/91 | Brandeis University, Waltham, MA. |
Research Experience
| 3/00-present | University of Rochester, Rochester, NY. Postdoctoral Research Associate. Advisor: Dr. Eric Phizicky |
| Function and Mechanism of the 2'-phosphotransferase that catalyzes the final step in tRNA splicing in Saccharomyces cerevisiae. Defining the rate-determining step for 2'-phosphate removal from RNA using steady-state and transient kinetic techniques to determine if additional cellular components act to enhance the slow rate of reaction that has been observed in vitro. Using RNA-interference to generate a knockout of 2'-phosphotransferase activity in Drosophila Melanogaster S2 cells to address the role of the enzyme in higher eukaryotes, which may splice tRNA's by a different pathway thus obviating the need for 2'-phosphotransferase activity in the production of mature tRNA's. | |
| 9/94 – 7/99 | Duke University, Durham, NC. Graduate Research Assistant. |
| 7/99 - 2/00 | Duke University, Durham, NC. Postdoctoral Research Associate. Advisors: Dr. Christian Raetz and Dr. Carol Fierke |
| Investigation of the metal ion requirement and inhibition of the UDP-3-O-acyl-GlcNac deacetylases (LpxC) from Escherichia coli and Aquifex aeolicus. Used steady-state kinetics measurements and spectroscopic techniques to demonstrate requirement for a single zinc ion by LpxC. Cloned and purified A. aeolicus LpxC and studied inhibition of these enzymes by substrate analog inhibitors. Used site-directed mutagenesis to identify potential zinc-coordinating residues in LpxC. | |
| 5/93 – 8/94 | University of Rochester, Rochester, NY. Undergraduate Research Assistant. Advisor: Dr. George McLendon |
| Assessed interactions and electron transfer between mutant S. cerevisiae Cytochrome c proteins and Cytochrome c Peroxidase. |
Honors/Awards
| 9/95 – 9/98 | National Science Foundation Predoctoral Fellowship |
| 9/94 – 9/97 | James B. Duke Graduate Fellowship, Duke University |
| 5/94 | Summa Cum Laude |
| 4/93 | Phi Beta Kappa Honor Society |
Publications
Jackman, J. E., Raetz, C. R. H., Fierke, C. A. (2001). Site-Directed Mutagenesis of the Bacterial Metalloamidase UDP-(3-O-acyl)-N-acetylglucosamine Deacetylase (LpxC). Identification of the Zinc Binding Site. Biochemistry, 40, 514-523.
Jackman, J. E., Fierke, C. A., Tumey, L. N., Pirrung, M., Uchiyama, T., Tahir, S. H., Hindsgaul, O., Raetz, C. R. H. (2000). UDP-3-O-acyl-GlcNAc Antibacterial Agents that Target Lipid A Biosynthesis in Gram-negative Bacteria. Inhibition of diverse UDP-3-O-acyl-N-acetylglucosamine deacetylases (LpxC’s) by substrate-analogs containing zinc-binding motifs. Journal of Biological Chemistry, 275; 11002-11009.
Jackman, J. E., Raetz, C. R. H., Fierke, C. A. (1999). UDP-3-O-(R-3-Hydroxymyristoyl)-N-acetylglucosamine Deacetylase of Escherichia coli is a Zinc Metalloenzyme. Biochemistry, 38: 1902-1911.
Ogura, T., Inoue, K., Tatsuta, T., Suzaki, T., Karata, K., Young, K., Su, L.-H., Fierke, C. A., Jackman, J. E., Raetz, C. R. H., Coleman, J., Tomoyasu, T., Matsuzawa, H. (1999). Balanced Biosynthesis of Major Membrane Components Through Regulated Degradation of the Committed Enzyme of Lipid A Biosynthesis by the AAA Protease FtsH (HflB) in Escherichia coli. Molecular Microbiology, 31:833-844.
Wyckoff, T. J. O., Raetz, C. R. H., Jackman, J. E. (1998). Antibacterial and Anti-inflammatory Agents that Target Endotoxin. Trends in Microbiology, 6:154-159.
Jackman, J. E., Merz, K. M., Fierke, C. A. (1996). Disruption of the Active Site Solvent Network in Carbonic Anhydrase II Decreases the Efficiency of Proton Transfer. Biochemistry, 35:16421-16428.
Invited presentations
Jackman, J. E., Raetz, C. R. H., Fierke, C. A. (1999). Determination of protein residues involved in binding the required zinc ion in the E. coli UDP-3-O-acyl-GlcNAc deacetylase. Graduate Gordon Research Conference- Bioinorganic Chemistry; Ventura, CA.
Papers presented
Jackman, J. E., Raetz, C. R. H., Fierke, C. A. (1999). A Thermostable Zinc Metalloenzyme: UDP-3-O-acyl-GlcNAc deacetylase from Aquifex aeolicus. Sixteenth Enzyme Mechanisms Conference; Napa, CA.
Jackman, J. E., Raetz, C. R. H., Fierke, C. A. (1998). A Single Zinc is Required for UDP-3-O-acyl-GlcNAc deacetylase activity. Annual Meeting of the American Society for Biochemistry and Molecular Biology; Washington, DC.