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Updated: Sep 23, 2026

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
Published on: November 22, 2014
Many paths to methyltransfer: a chronicle of convergence
Heidi L Schubert1, Robert M Blumenthal, Xiaodong Cheng
1Department of Biochemistry, University of Utah, Salt Lake City 84132-3201, USA. heidi@biochem.utah.edu
Abstract:
S-adenosyl-L-methionine (AdoMet) dependent methyltransferases (MTases) are involved in biosynthesis, signal transduction, protein repair, chromatin regulation and gene silencing. Five different structural folds (I-V) have been described that bind AdoMet and catalyze methyltransfer to diverse substrates, although the great majority of known MTases have the Class I fold. Even within a particular MTase class the amino-acid sequence similarity can be as low as 10%. Thus, the structural and catalytic requirements for methyltransfer from AdoMet appear to be remarkably flexible.
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