About the Scientist
Training
| Degree: |
Ph.D. |
| Institution: |
University of British Columbia |
| Year: |
2006 |
|
| Degree: |
B.Sc. (Pharm) |
| Institution: |
University of British Columbia |
| Year: |
1999 |
|
Current Position
| Position: |
Post-Doctoral Fellow |
| Research Group: |
Adam Frankel's Lab |
| Supervisors: |
Dr. Adam Frankel |
|
|
Scholarships + Awards
| Name: |
Merck Frosst Postgraduate Pharmacy Fellowship |
|
|
| Name: |
University Graduate Fellowship |
| Organization: |
University of British Columbia |
|
|
| Name: |
Frosst Pharmacy Scholarship |
|
|
Links
About The Research
Post-translational modification of proteins increase the diversity of protein structure and add to the already diverse symphony of signals that drives biological processes. Arginine methylation is one such modification catalyzed by protein arginine N-methyltransferases (PRMTs). These enzymes transfer methyl groups from the co-substrate S-adenosyl-L-methionine to the arginine residues within proteins. The addition of methyl groups disrupts the hydrogen-bonding capacity of arginine residues without affecting its positive electrostatic charge. This modification has been shown to control processes that include transcription, RNA processing, DNA repair, and viral replication.
We investigate the substrate specificity, kinetic activity, and inhibition of PRMTs. We are also interested in protein-protein interactions that augment or hinder enzymatic activity. We hope that this and other studies will lead to a greater understanding of the mechanisms of PRMTs and we hope to use this understanding will lead to the development of novel inhibitors of PRMTs.
Publications + Presentations
| Publications |
- Lakowski TM, Zurita-Lopez C, Clarke SG, and Frankel A. Approaches to measuring the activities of protein arginine N-methyltransferases. Analytical Biochemistry. 2009 (Accepted, in press).
- Lakowski TM, Frankel A. Sources of AdoHcy background in measuring PRMT activity using tandem mass spectrometry. Analytical Biochemistry. 2009 (Accepted, in press).
- Lakowski TM, Frankel A. Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4. Biochemical Journal. 2009 Jun. 26: 421(2): 253-61. (Cover article)
- Lakowski TM, Frankel A. A kinetic study of human protein arginine N-methyltransferase 6 reveals a distributive mechanism. Journal of Biological Chemistry. 2008 April 11; 283(15): 10015-25.
- Lakowski TM, Frankel A. A kinetic study of human protein arginine N-methyltransferase 6 reveals a distributive mechanism. Journal of Biological Chemistry. 2008 April 11; 283(15): 10015-25.
- Lakowski TM, Lee GM, Okon M, Reid RE, McIntosh LP. Calcium-induced folding of a fragment of calmodulin composed of EF-hands 2 and 3. Protein Science. 2007 Jun;16(6): 1119-32. (Cover article)
|
« Back
