DIFFERENTIAL POST-TRANSLATIONAL MODIFICATION OF HUMAN TYPE-I KERATINS SYNTHESIZED IN A RABBIT RETICULOCYTE CELL-FREE SYSTEM
DIFFERENTIAL POST-TRANSLATIONAL MODIFICATION OF HUMAN TYPE-I KERATINS SYNTHESIZED IN A RABBIT RETICULOCYTE CELL-FREE SYSTEM
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DOI：
10.1016/0167-4781(85)90055-7
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发表时间：
1985-01-01
期刊：
影响因子：
--
通讯作者：
FREEDBERG, IM
中科院分区：
文献类型：
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作者：
GIBBS, PEM;ZOUZIAS, DC;FREEDBERG, IM
在兔网织红细胞裂解物系统中合成的翻译产物，从总细胞mRNA从人上皮细胞系ME-180，进行了检查。角蛋白在这些翻译产物中是突出的，它们与从细胞中纯化的角蛋白在十二烷基硫酸钠-聚丙烯酰胺凝胶中精确地结合。在体内乙酰化的I型酸性角蛋白也被网织红细胞裂解物乙酰化。通过已知在体内被磷酸化的2种酸性角蛋白的二维电泳检查揭示，这些蛋白质中只有一种在裂解物系统中被磷酸化。这种蛋白质的磷酸化发生在完整的多肽链从核糖体释放之后。已知由裂解物磷酸化的蛋白质是唯一由cAMP调节的ME-180磷酸角蛋白，反映了ME-180角蛋白在体内的体外差异修饰。
The translation products synthesized in a rabbit reticulocyte lysate system, from total cellular mRNA from the human epithelial cell-line ME-180, were examined. Keratin proteins are prominent among these translation products, and they precisely coelectrophorese in sodium dodecyl sulfate-polyacrylamide gels with keratins purified from the cells. Type-I, acidic, keratins which are acetylated in vivo, are also acetylated by the reticulocyte lysate. Examination by 2-dimensional electrophorsis of 2 acidic keratins known to be phosphorylated in vivo reveals that only one of these proteins is phosphorylated in the lysate system. Phosphorylation of this protein occurs after release of the completed polypeptide chain from the ribosome. The protein phosphorylated by the lysate is known to be the only ME-180 phosphokeratin modulated by cAMP, reflecting in vitro the differential modification of ME-180 keratins in vivo.