Semliki森林病毒p62蛋白的信号序列参与起始过程，但不参与链转位的完成。
The signal sequence of the p62 protein of Semliki Forest virus is involved in initiation but not in completing chain translocation.
作者信息
Garoff H, Huylebroeck D, Robinson A, Tillman U, Liljeström P
机构信息
Department of Molecular Biology, Karolinska Institute, Huddinge, Sweden.
出版信息
J Cell Biol. 1990 Sep;111(3):867-76. doi: 10.1083/jcb.111.3.867.
Abstract
So far it has been demonstrated that the signal sequence of proteins which are made at the ER functions both at the level of protein targeting to the ER and in initiation of chain translocation across the ER membrane. However, its possible role in completing the process of chain transfer (see Singer, S. J., P. A. Maher, and M. P. Yaffe. Proc. Natl. Acad. Sci. USA. 1987. 84:1015-1019) has remained elusive. In this work we show that the p62 protein of Semliki Forest virus contains an uncleaved signal sequence at its NH2-terminus and that this becomes glycosylated early during synthesis and translocation of the p62 polypeptide. As the glycosylation of the signal sequence most likely occurs after its release from the ER membrane our results suggest that this region has no role in completing the transfer process.
摘要
到目前为止，已经证明在内质网合成的蛋白质的信号序列在蛋白质靶向内质网水平以及启动跨内质网膜的链转位过程中均发挥作用。然而，其在完成链转移过程中的可能作用（见辛格，S. J.，P. A. 马赫，和 M. P. 亚夫。《美国国家科学院院刊》。1987年。84:1015 - 1019）仍然难以捉摸。在这项工作中，我们表明塞姆利基森林病毒的p62蛋白在其NH2末端含有一个未切割的信号序列，并且该序列在p62多肽的合成和转位早期就发生了糖基化。由于信号序列的糖基化很可能在其从内质网膜释放后发生，我们的结果表明该区域在完成转移过程中没有作用。
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