Clustering of glycine and NG,NG-dimethylarginine in nucleolar protein C23.
Protein C23 (Mr 110 000, pI = 5.5), a major phosphoprotein in the nucleolus of mammalian cells, has been shown to contain 1.3 mol% of NG,NG-dimethylarginine (DMA) [Lischwe, M.A., Roberts, K.D., Yeoman, L.C., & Busch, H. (1982) J. Biol. Chem. 257, 14600-14602]. A tryptic peptide from protein C23 that contains DMA has been isolated and sequenced. Its sequence is Gly-Glu-Gly-Gly-Phe-Gly-Gly-DMA-Gly-Gly-Gly-DMA-Gly-Gly-Phe-Gly-Gly-DMA- Gly-Gly- Gly-DMA-Gly-Gly-DMA-Gly-Gly-Phe-Gly-Gly-DMA-Gly-DMA-Gly-Gly-Phe-Gly-Gly- DMA-Gly-Gly-Phe-DMA-Gly-Gly-DMA-Gly-Gly-Gly-Gly-Asp-Phe-Lys. This peptide contains 34 glycine, 10 DMA, and 6 phenylalanine residues and has clusters of glycine and NG,NG-dimethylarginine interspersed with phenylalanine residues. A similar domain has been found at the amino terminus of a nucleolar protein of Mr 34,000, pI = 8.5. This sequence array may represent a conserved domain characteristic of a certain class of nuclear proteins. All of the methylated arginine residues in protein C23, the 34-kilodalton protein, and myelin basic protein [Carnegie, P.R. (1971) Biochem. J. 123, 57-67] have at least one adjacent glycine. Access of certain arginine methylases to arginine residues may be sterically possible because of the lack of a side chain on the adjacent glycine residue(s).
D000595:Amino Acid Sequence; D000818:Animals; D001120:Arginine / Q000031:analogs & derivatives* / Q000032:analysis; D005998:Glycine / Q000032:analysis*; D008114:Liver Neoplasms, Experimental / Q000032:analysis; D008970:Molecular Weight; D009687:Nuclear Proteins; D000090243:Nucleophosmin; D010446:Peptide Fragments / Q000032:analysis; D051381:Rats; D012261:Ribonucleoproteins / Q000302:isolation & purification; D013329:Structure-Activity Relationship; D014357:Trypsin
D009687:Nuclear Proteins; D010446:Peptide Fragments; D012261:Ribonucleoproteins; D000090243:Nucleophosmin; C018524:N,N-dimethylarginine; D001120:Arginine; D014357:Trypsin; D005998:Glycine