CLUSTERING OF GLYCINE AND NG,NG-DIMETHYLARGININE IN NUCLEOLAR PROTEIN-C23
CLUSTERING OF GLYCINE AND NG,NG-DIMETHYLARGININE IN NUCLEOLAR PROTEIN-C23
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DOI：
10.1021/bi00343a001
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发表时间：
1985-01-01
期刊：
影响因子：
2.9
通讯作者：
BUSCH, H
中科院分区：
文献类型：
--
作者：
LISCHWE, MA;COOK, RG;BUSCH, H
蛋白质C23（Mr 110 000，pI = 5.5）是哺乳动物细胞核仁中的主要磷蛋白，已显示含有1.3mol%的NG，NG-二甲基精氨酸（DMA）[Lische，M.A.，罗伯茨，K. D.，Yeoman，L.C.和Busch，H.（1982）J.Biol.Chem.257，14600-14602]。从含有DMA的蛋白质C23的胰蛋白酶肽已被分离和测序。其序列为Gly-Glu-Gly-Gly-Phe-Gly-Gly-DMA-Gly-Gly-Phe-Gly-Gly-DMA-Gly-Gly-Gly-Gly-DMA-Gly-Gly-DMA-Gly-Gly-Phe-Gly-Gly-DMA-Gly-Gly-Phe-DMA-Gly-Gly-Gly-Gly-DMA-Gly-Gly-Gly-Gly-ASP-Phe-Lys。该肽含有34个甘氨酸、10个DMA和6个苯丙氨酸残基，并且具有散布有苯丙氨酸残基的甘氨酸和NG、NG-二甲基精氨酸簇。一个类似的结构域已被发现在氨基末端的核仁蛋白的Mr 34 000，pI = 8.5。该序列阵列可能代表了某类核蛋白的保守结构域特征。蛋白C23、34千道尔顿蛋白和髓鞘碱性蛋白中的所有甲基化精氨酸残基[Carnegie，P.R.（1971）Biochem.J.123，57-67]具有至少一个相邻的甘氨酸。某些精氨酸甲基化酶接近精氨酸残基在空间上是可能的，因为在相邻的甘氨酸残基上缺乏侧链。
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) [Lische, M.A., Roberts, K.D., Yeoman, L.C. and 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 certai arginine methylases to argine residues may be sterically possible because of the lack of a side chain on the adjacent glycine residue(s).