Chang D, Haynes J I, Brady J N, Consigli R A
Division of Biology, NSCORT, Kansas State University, Manhattan 66506, USA.
Trans Kans Acad Sci. 1993 Apr;96(1-2):35-9.
The molecular mechanism participating in the transport of newly synthesized proteins from the cytoplasm to the nucleus in mammalian cells is poorly understood. Recently, the nuclear localization signal sequences (NLS) of many nuclear proteins have been identified, and most have been found to be composed of a highly basic amino acid stretch. A genetic "subtractive" and a biochemical "additive" approach were used in our studies to identify the NLS's of the polyomavirus structural capsid proteins. An NLS was identified at the N-terminus (Ala1-Pro-Lys-Arg-Lys-Ser-Gly-Val-Ser-Lys-Cys11) of the major capsid protein VP1 and at the C-terminus (Glu307 -Glu-Asp-Gly-Pro-Glu-Lys-Lys-Lys-Arg-Arg-Leu318) of the VP2/VP3 minor capsid proteins.
哺乳动物细胞中参与将新合成蛋白质从细胞质转运至细胞核的分子机制目前仍知之甚少。最近，许多核蛋白的核定位信号序列（NLS）已被鉴定出来，并且发现大多数由高度碱性的氨基酸序列组成。我们的研究采用了遗传“减法”和生化“加法”方法来鉴定多瘤病毒结构衣壳蛋白的NLS。在主要衣壳蛋白VP1的N端（Ala1 - Pro - Lys - Arg - Lys - Ser - Gly - Val - Ser - Lys - Cys11）和VP2/VP3次要衣壳蛋白的C端（Glu307 - Glu - Asp - Gly - Pro - Glu - Lys - Lys - Lys - Arg - Arg - Leu318）鉴定出了一个NLS。
