title: DNA methyltransferase-moderated click chemistry.
abstract: [reaction: see text]. Biological methylation plays a vital role in regulatory mechanisms of gene transcription. Methylation of both promoter sequences within the genome, as well as protein substrates, has a profound impact upon gene transcription. Yet, few tools exist by which to identify sites of biological methylation in complex biological mixtures. We have generated a novel adenosine-derived N-mustard that serves as an efficient synthetic cofactor and allows for subsequent "click" chemistry involving the modified nucleic acid substrate.
authors.affiliation: Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53705, USA.
authors.forename: Rachel L
authors.initials: RL
authors.lastname: Weller
authors.forename: Scott R
authors.initials: SR
authors.lastname: Rajski
mesh_terms: D000241:Adenosine / Q000031:analogs & derivatives / Q000737:chemistry*; D001483:Base Sequence; D002621:Chemistry / Q000379:methods*; D003500:Cyclization; D004247:DNA / Q000737:chemistry*; D015254:DNA Modification Methylases / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D008745:Methylation; D015394:Molecular Structure
chemical_list: D004247:DNA; D015254:DNA Modification Methylases; D000241:Adenosine