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莫洛尼氏鼠肉瘤病毒的转化蛋白是一种可溶性细胞质蛋白。

The transforming protein of Moloney murine sarcoma virus is a soluble cytoplasmic protein.

作者信息

Papkoff J, Nigg E A, Hunter T

出版信息

Cell. 1983 May;33(1):161-72. doi: 10.1016/0092-8674(83)90345-8.

Abstract

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, we have determined the subcellular location of p37mos in M-MuSV 124-transformed cells. Using two different methods of cell lysis and fractionation, we 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.

摘要

莫洛尼氏鼠肉瘤病毒(M-MuSV)的转化基因v-mos编码一种37000道尔顿的磷蛋白,即p37mos。由于该蛋白的生化功能尚不清楚,我们确定了p37mos在M-MuSV 124转化细胞中的亚细胞定位。使用两种不同的细胞裂解和分级分离方法,我们发现新合成的以及成熟的p37mos都是可溶性细胞质蛋白。与这些结果一致,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,产生了弥漫性细胞质模式。凝胶过滤实验和甘油梯度沉降分析表明,大部分p37mos以单体形式存在,不参与与其他细胞蛋白的特异性结合。p37mos的这些特性与其他已表征的逆转录病毒转化蛋白不同。

相似文献

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Serine kinase activity associated with Maloney murine sarcoma virus-124-encoded p37mos.
Virology. 1985 May;143(1):321-33. doi: 10.1016/0042-6822(85)90119-9.
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Recognition of mos-related proteins with an antiserum to a peptide of the v-mos gene product.
J Gen Virol. 1985 May;66 ( Pt 5):945-55. doi: 10.1099/0022-1317-66-5-945.

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