Many paths to methyltransfer: a chronicle of convergence

• Type of Material: Article
• Authors: Heidi L. Schubert, University of Utah; Robert M. Blumenthal, Medical College of Ohio; Xiaodong Cheng, Emory University
• Language: English
• Date: 2003-06
• Publisher: Elsevier (Cell Press)
• Publication Version: Author Accepted Manuscript (After Peer Review)
• Copyright Statement: © 2003 Elsevier Science Ltd. All rights reserved.
• License: Creative Commons Attribution-NonCommerical-NoDerivs 3.0 Unported
• Final Published Version (URL): http://dx.doi.org/10.1016/S0968-0004(03)00090-2
• Title of Journal or Parent Work: Trends in Biochemical Sciences
• ISSN: 0968-0004
• Volume: 28
• Issue: 6
• Start Page: 329
• End Page: 335
• Grant/Funding Information: H.L.S. was supported by grants from NIH (GM56775 and DK02794), R.M.B. was supported by a grant from the U.S. National Science Foundation (MCB-9904523), and X.C. was supported by NIH (GM49245 and GM61355) and the Georgia Research Alliance.; National Institute of General Medical Sciences : NIGMS
• Research Categories: Chemistry, Biochemistry

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.