myelin-basic-protein and methylamine

The novel post-translationally modified residue gamma-N-methylasparagine, previously detected in the beta subunit of allophycocyanin (Klotz, A. V., Leary, J. A., and Glazer, A. N. (1986) J. Biol. Chem. 261, 15891-15894), has been found in the beta subunits of a variety of other phycobiliproteins. Representatives of C- and R-phycocyanins and B-, C-, and R-phycoerythrins all contain 1 eq of gamma-N-methylasparagine on their beta subunits as judged by the presence of methylamine in acid hydrolysates. Radiotracer experiments show that the methyl group is derived from the S-methyl of methionine, implicating S-adenosylmethionine as an intermediate methyl transfer agent. Isolation of peptides from C-phycocyanins, prepared from cells labeled by L-[methyl-14C]methionine, showed that the gamma-N-methylasparagine residue is at position beta-72, within a highly conserved region in phycobiliproteins. This location corresponds to that reported earlier for the position of gamma-N-methylasparagine in allophycocyanin and R-phycoerythrin. Phycobiliprotein alpha subunits contain insignificant amounts of the adduct. Methylamine is absent from the hydrolysates of the beta subunits or alpha beta monomers of phycobiliproteins from certain organisms. These latter data indicate that the gamma-N-methylasparagine residue is dispensable in some circumstances. The function of this modification remains to be established. gamma-N-methylasparagine was also absent from several other proteins including bovine histones, porcine myelin basic peptide, and the Salmonella typhimurium aspartate chemoreceptor, all known to undergo post-translational methylations.

Topics: Amino Acid Sequence; Animals; Asparagine; Histones; Light-Harvesting Protein Complexes; Methylamines; Myelin Basic Protein; Plant Proteins; Protein Processing, Post-Translational