FASEB Conference on Biological Methylation: July 17-22, 1999, Vermont Academy, Saxton's River, VT

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BlumenthalEnzymatic transmethylation of molecules from the highly abundant methyl donor S-adenosyl-L-methionine (AdoMet) presents a paradox. On the one hand, AdoMet-dependent methylation is central to everything from metal detoxification through biosynthesis to gene regulation via DNA methylation. Analysis of genome sequences from archaea, eubacteria, fungi, plants and animals suggests that a surprisingly large fraction of all genes specify AdoMet-dependent methyltransferases. On the other hand, remarkably little is known about this important and diverse group of enzymes. For example, it was only four years ago that the first structure of an AdoMet-dependent enzyme was reported. Since that time, it has been found that almost all characterized AdoMet-dependent methyltransferases share a common core structure despite having virtually undetectable sequence identity and despite methylating substrates as different as catechol and DNA. In terms of biological importance and the potential for providing basic insights into structure-function relationships and enzyme evolution, the AdoMet-dependent enzymes appear to be ripe for intensified investigation.From July 17 through July 22, 1999, the Federation of American Societies for Experimental Biology (FASEB) is sponsoring the fourth biennial summer research conference on Biological Methylation. These meetings are virtually unique in their focus on the full range of AdoMet-dependent methyltransferases, a diverse set of enzymes of broad biological function and importance. The conferences are held at the Vermont Academy in Saxtons River, VT, and attract an international group of participants.