Dr. Robert Neely, School of Chemistry, University of Birmingham
Tuesday 10th May, 1.00 p.m., Stacey Lecture Theatre 1
Thousands of protein, RNA and DNA methyltransferase enzymes exist in nature and all catalyse the transfer of a methyl-group from the ubiquitous cofactor, S-adenosyl-l-methionine, to their target. These enzymes are proving to be a remarkably malleable1. Their ability to catalyze reactions goes far beyond methyl-transfer and we are now able to use them to catalyse the transfer of much more bulky and useful groups to their target sites on DNA, RNA and proteins.
Recent work in my lab has focused on the application of the methyltransferases in optical DNA mapping2. Here, we have been using DNA methyltransferases to catalyse the transfer of fluorophores to DNA. The site-specific fluorophore transfer enables us to visualize DNA sequence in a unique way, analogous to a barcode. In this way, we can collect data on thousands of long DNA molecules in a matter of minutes. Furthermore, the data is inherently single molecule, so we derive a quantitative description of the genomic content of a sample.
I will discuss recent work on exploring the scope and efficiency of the methyltransferase-catalysed labeling reaction and give a brief overview of future direction for this technology.
- Dalhoff,C., Lukinavicius,G., Klimasauskas,S. and Weinhold,E. (2006). Nat Chem Biol, 2, 31–32.
- Vranken,C., Deen,J., Dirix,L., Stakenborg,T., Dehaen,W., Leen,V., Hofkens,J. and Neely,R.K. (2014). Nucleic Acids Res., 42, e50–e50.