Jj. Smith et al., Unusual sites of arginine methylation in poly(A)-binding protein II and invitro methylation by protein arginine methyltransferases PRMT1 and PRMT3, J BIOL CHEM, 274(19), 1999, pp. 13229-13234
Arginine methylation is a post-translational modification found mostly in R
NA-binding proteins. Poly(A) binding protein II from calf thymus was shown
by mass spectrometry and sequencing to contain N-G-N-G-dimethylarginine at
13 positions in its amino acid sequence. Two additional arginine residues w
ere partially methylated. Almost all of the modified residues were found in
Arg-Xaa-Arg clusters in the C terminus of the protein. These motifs are di
stinct from Arg-Gly-Gly motifs that have been previously described as sites
and specificity determinants for asymmetric arginine dimethylation. Poly(A
)-binding protein II and deletion mutants expressed in Escherichia coil wer
e in vitro substrates for two mammalian protein arginine methyltransferases
, PRMT1 and PRMT3, with S-adenosyl-L-methionine as the methyl group donor.
Both PRMT1 and PRMT3 specifically methylated arginines in the C-terminal do
main corresponding to the naturally modified sites.