Pawson T, Guyden J, Kung T H, Radke K, Gilmore T, Martin G S
Cell. 1980 Dec;22(3):767-75. doi: 10.1016/0092-8674(80)90553-x.
Cells infected by one strain of Fujinami sarcoma virus (FSV) are transformed at 38 degrees C but are phenotypically normal at 41.5 degrees C. FSV encodes a 140,000 molecular weight protein (P140) with gag gene-related and FSV-specific peptide sequences. At 41.5 degrees C, P140 is weakly phosphorylated at serine residues, and is inactive in the immune complex protein kinase assay. At 38 degrees C, P140 is highly phosphorylated, contains phosphotyrosine in addition to phosphoserine, and in the immune complex kinase assay becomes phosphorylated at three tyrosine residues. Phosphorylation of cellular polypeptides at tyrosine residues in FSV-infected cells is also temperature-sensitive. These observations indicate that P140 is the transforming protein of FSV and that protein phosphorylation at tyrosine residues is involved in transformation by this virus.
被一种 Fujinami 肉瘤病毒(FSV)感染的细胞在 38 摄氏度时发生转化,但在 41.5 摄氏度时表型正常。FSV 编码一种分子量为 140,000 的蛋白质(P140),其具有与 gag 基因相关的和 FSV 特异性的肽序列。在 41.5 摄氏度时,P140 在丝氨酸残基处弱磷酸化,并且在免疫复合物蛋白激酶测定中无活性。在 38 摄氏度时,P140 高度磷酸化,除了磷酸丝氨酸外还含有磷酸酪氨酸,并且在免疫复合物激酶测定中在三个酪氨酸残基处被磷酸化。FSV 感染细胞中细胞多肽在酪氨酸残基处的磷酸化也是温度敏感的。这些观察结果表明 P140 是 FSV 的转化蛋白,并且酪氨酸残基处的蛋白质磷酸化参与了该病毒的转化过程。