1 Protein methyltransferases: Their distribution among the five structural classes of adomet-dependent methyltransferases

Heidi L. Schubert, Robert M. Blumenthal, Xiaodong Cheng

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

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 (designated I through 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. MTases that act on protein substrates have been found to date among three of the five structural classes (I, the classical fold; III, the corrin MTase fold; and V, the SET fold). "There are many paths to the top of the mountain, but the view is always the same."-Chinese proverb The Columbia World of Quotations, New York, Columbia University Press, 1996.

Original languageEnglish (US)
Pages (from-to)3-28
Number of pages26
JournalEnzymes
Volume24
Issue numberC
DOIs
StatePublished - 2006
Externally publishedYes

ASJC Scopus subject areas

  • Biotechnology
  • Biophysics
  • Biochemistry
  • Molecular Biology

Fingerprint

Dive into the research topics of '1 Protein methyltransferases: Their distribution among the five structural classes of adomet-dependent methyltransferases'. Together they form a unique fingerprint.

Cite this