Sompayrac L, Danna K J
Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder 80309.
Virology. 1988 Apr;163(2):391-6. doi: 10.1016/0042-6822(88)90279-6.
We have constructed a new SV40 mutant, T147, that makes a large T antigen that is only 147 amino acids long. We show that the T147 T antigen is a phosphoprotein that is as stable as wild-type T antigen and that the SV40 viral origin binding activity of the T147 T antigen is reduced at least 100-fold relative to that of wild-type T antigen. Most importantly, we demonstrate that cloned T147 DNA transforms rat F111 cells to anchorage independence as efficiently as cloned wild-type SV40 DNA and that cloned T147 DNA also efficiently transforms C3H10T1/2 mouse cells in a focus assay.
我们构建了一种新的SV40突变体T147，它产生的大T抗原仅由147个氨基酸组成。我们发现T147 T抗原是一种磷蛋白，其稳定性与野生型T抗原相同，并且T147 T抗原的SV40病毒起源结合活性相对于野生型T抗原降低了至少100倍。最重要的是，我们证明克隆的T147 DNA转化大鼠F111细胞使其不依赖贴壁生长的效率与克隆的野生型SV40 DNA相同，并且在焦点试验中克隆的T147 DNA也能有效地转化C3H10T1/2小鼠细胞。
