Müller R, Bravo R, Müller D, Kurz C, Renz M
European Molecular Biology Laboratory, Heidelberg, Fed. Rep. of Germany.
Oncogene Res. 1987;2(1):19-32.
We have studied the biosynthesis and biochemical properties of the c-fos gene product and its associated protein (p39) in growth factor-stimulated fibroblasts. c-fos is a markedly acidic protein that is extensively post-translationally modified by phosphorylation and another type of modification not changing its relative molecular mass (Mr). More than 10 different forms of c-fos protein can be identified by two-dimensional gel analysis. In c-fos-transformed cells, however, most of the highly modified forms are missing. The affinity for DNA of less phosphorylated c-fos-protein complexes is higher than that of the highly modified ones. The transforming potential of c-fos protein and its affinity for DNA thus seems to be inversely correlated with the extent of its phosphorylation. In contrast to c-fos, p39 is a basic protein that is rendered even more basic by post-translational modification. Two other forms of p39 differing in specific domains of the protein (p41 and p43) were also found to be complexed with c-fos.
我们研究了生长因子刺激的成纤维细胞中c-fos基因产物及其相关蛋白（p39）的生物合成和生化特性。c-fos是一种酸性很强的蛋白质，在翻译后会被磷酸化以及另一种不改变其相对分子质量（Mr）的修饰广泛修饰。通过二维凝胶分析可鉴定出10多种不同形式的c-fos蛋白。然而，在c-fos转化的细胞中，大多数高度修饰的形式缺失。磷酸化程度较低的c-fos蛋白复合物对DNA的亲和力高于高度修饰的复合物。因此，c-fos蛋白的转化潜力及其对DNA的亲和力似乎与其磷酸化程度呈负相关。与c-fos相反，p39是一种碱性蛋白，翻译后修饰使其碱性更强。还发现另外两种在蛋白质特定结构域不同的p39形式（p41和p43）与c-fos复合。
