THE TRANSFORMING PROTEIN OF MOLONEY MURINE SARCOMA-VIRUS IS A SOLUBLE CYTOPLASMIC PROTEIN
THE TRANSFORMING PROTEIN OF MOLONEY MURINE SARCOMA-VIRUS IS A SOLUBLE CYTOPLASMIC PROTEIN
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DOI：
10.1016/0092-8674(83)90345-8
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发表时间：
1983-01-01
期刊：
影响因子：
64.5
通讯作者：
HUNTER, T
中科院分区：
文献类型：
--
作者：
PAPKOFF, J;NIGG, EA;HUNTER, T
莫洛尼鼠肉瘤病毒（Moloney murine sarcoma virus，M-MuSV）的转化基因v-mos编码一个37，000-道尔顿的磷蛋白p37 mos。由于这种蛋白的生化功能是未知的，在M-MuSV 124转化的小鼠细胞中确定了p37 mos的亚细胞定位。使用2种不同的细胞裂解和分级分离方法，发现新合成的以及成熟的p37 mos是可溶性胞质蛋白。与这些结果一致，使用针对合成v-mos肽的抗血清对急性感染M-MuSV 124的细胞进行免疫荧光染色，产生弥散的细胞质模式。凝胶过滤实验和甘油梯度沉降分析表明，大部分的p37 mos作为单体存在，并不参与与其他细胞蛋白的特定关联。p37 mos的这些特性不同于其他特征性逆转录病毒转化蛋白的特性。
The transforming gene, v-mos, of Moloney murine sarcoma virus (M-MuSV) encodes a 37,000-dalton phosphoprotein, p37mos. Since the biochemical function of this protein is unknown, the subcellular location of p37mos was determined in M-MuSV 124-transformed mouse cells. Using 2 different methods of cell lysis and fractionation, it was found that newly synthesized as well as mature p37mos is a soluble cytoplasmic protein. In agreement with these results, immunofluorescent staining of cells acutely infected with M-MuSV 124, using an antiserum directed against a synthetic v-mos peptide, produced a diffuse cytoplasmic pattern. Gel filtration experiments and glycerol gradient sedimentation analysis suggest that the bulk of p37mos exists as a monomer and is not involved in a specific association with other cellular proteins. These properties of p37mos are different from those of other characterized retroviral transforming proteins.