A basic protein from the dimorphic fungus Mucor racemosus, found to be highly methylated, is shown to be protein synthesis elongation factor la. This protein is the most abundant protein in hyphal cells but is less abundant in yeast cells. It is posttranslationally methylated with the formation of mono-, di-, and trimethyllysine at as many as 16 sites. Nearly 20% of the 44 lysine residues of elongation factor la from mycelia are modified while those from sporangiospores are virtually unmethylated.Mucor racemosus is a dimorphic fungus that exists in either yeast or hyphal forms. These changes in morphology are accompanied by changes in the translational system, evidenced by an acceleration in the rate of peptide bond formation (1, 2) and by a change in the level of phosphorylation of a ribosomal protein (3). In the course of studying posttranslational modifications in the fungus, we resolved several methylated peptides by using two-dimensional polyacrylamide gel electrophoresis. We have now identified one of these peptides as the a subunit of protein synthesis elongation factor 1 (EF-la), the functional equivalent of prokaryotic elongation factor Tu (EF-Tu) (4). EFTu from Salmonella typhimurium and Escherichia coli is methylated (5, 6), and that in E. coli contains a single methyllysine at position 56.In certain proteins, acidic amino acids are methylated by a reversible carboxymethylation reaction, examples of which have been shown to play roles in bacterial chemotaxis (7-9), leukocyte chemotaxis (10-12), and hormone secretion (13). The methylation of basic amino acids occurs at the E-amino group of lysine, the guanidinium group of arginine, or the imidazole group of histidine (14). Although these reactions show a high degree of specificity, there has been no clear functional role assigned to the presence ofmethylated basic amino acids. Methylated basic amino acids occur in histones (15,16,17)