The nucleolar protein, B-36, contains a glycine and dimethylarginine-rich sequence conserved in several other nuclear RNA-binding proteins.
The amino terminal sequence of the 34 kD nucleolar protein B-36 isolated from the slime mold Physarum polycephalum has been determined. This portion of B-36 is rich in glycine, phenylalanine and the modified amino acid asymmetrical dimethylarginine (DMA) and is 65% identical to that for fibrillarin, a similar and potentially homologous 34 kD nucleolar protein from rat. The terminus of B-36 contains an interesting nine amino acid sequence, Gly-DMA-Gly-Gly-Phe-Gly-Gly-DMA-Gly, which is precisely repeated three times in the 110 kD nucleolar protein nucleolin. Similar sequences have also been reported in a yeast nucleolar protein (SSB-1) and several hnRNP proteins (rat A1 and brine shrimp GRP33). The conserved nature of this unusual sequence is suggestive of an important function which may include RNA-binding since several of these proteins share this feature.
D000595:Amino Acid Sequence; D001120:Arginine / Q000031:analogs & derivatives* / Q000032:analysis; D002352:Carrier Proteins / Q000032:analysis*; D005998:Glycine / Q000032:analysis*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009687:Nuclear Proteins / Q000032:analysis*; D010804:Physarum / Q000032:analysis; D011497:Protein O-Methyltransferase; D016601:RNA-Binding Proteins
D002352:Carrier Proteins; D009687:Nuclear Proteins; D016601:RNA-Binding Proteins; C018524:N,N-dimethylarginine; D001120:Arginine; D011497:Protein O-Methyltransferase; C489179:nucleolar protein B-36, Physarum polycephalum; D005998:Glycine