title: 7 Non-histone protein lysine methyltransferases: Structure and catalytic roles.
abstract: Non-histone protein lysine methyltransferases (PKMTs) represent an exceptionally diverse and large group of PKMTs. Even accepting the possibility of multiple protein substrates, if the number of different proteins with methylated lysyl residues and the number of residues modified is indicative of individual PKMTs there are well over a hundred uncharacterized PKMTs. Astoundingly, only a handful of PKMTs have been studied, and of these only a few with identifiable and well-characterized structure and biochemical properties. Four representative PKMTs responsible for trimethyllysyl residues in ribosomal protein LI 1, calmodulin, cytochrome c, and Rubisco are herein examined for enzymological properties, polypeptide substrate specificity, functional significance, and structural characteristics. Although representative of non-histone PKMTs, and enzymes for whichcollectively there is a large amount of information, individually each of the PKMTs discussed in this chapter suffers from a lack of at least some critical information. Other than the obvious commonality in the AdoMet substrate cofactor and methyl group transfer, these enzymes do not have common structural features, polypeptide substrate specificity, or protein sequence. However, there may be a commonality that supports the hypothesis that methylated lysyl residues act as global determinants regulating specific protein-protein interactions.
authors.affiliation: Department of Horticulture University of Kentucky 407 Plant Science Building Lexington, KY 40546, USA.
authors.forename: Lynnette M A
authors.initials: LM
authors.lastname: Dirk
authors.affiliation: Department of Biological Chemistry University of Michigan Medical School Medical Science Building 1 Ann Arbor, MI 48109, USA.
authors.forename: Raymond C
authors.initials: RC
authors.lastname: Trievel
authors.affiliation: Department of Horticulture University of Kentucky 407 Plant Science Building Lexington, KY 40546, USA.
authors.forename: Robert L
authors.initials: RL
authors.lastname: Houtz