SEC61P IS ADJACENT TO NASCENT TYPE-I AND TYPE-II SIGNAL-ANCHOR PROTEINS DURING THEIR MEMBRANE INSERTION
SEC61P IS ADJACENT TO NASCENT TYPE-I AND TYPE-II SIGNAL-ANCHOR PROTEINS DURING THEIR MEMBRANE INSERTION
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DOI：
10.1083/jcb.121.4.743
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发表时间：
1993-05-01
影响因子：
7.8
通讯作者：
DOBBERSTEIN, B
中科院分区：
文献类型：
--
作者：
HIGH, S;ANDERSEN, SSL;DOBBERSTEIN, B
我们已经鉴定出在I型和II型信号锚定蛋白插入内质网膜过程中与其相邻的膜成分。通过两种不同的交联方法，发现一种37 - 38kD的非糖基化蛋白（先前被鉴定为P37，High, S., D. Gorlich, M. Wiedmann, T. A. Rapoport和B. Dobberstein，1991年，《细胞生物学杂志》113卷：35 - 44页）与本研究中使用的所有插入膜的新生链相邻。基于免疫沉淀，这种内质网蛋白被证明与最近鉴定的哺乳动物Sec61蛋白相同。因此，Sec61p是I型和II型信号锚定蛋白在膜插入过程中（本研究）以及分泌蛋白在易位过程中（Gorlich, a, S. Prehn, E. Hartmann, K. - U. Kalies和T. A. Rapoport，1992年，《细胞》71卷：489 - 503页）的主要交联伙伴。我们提出，两种取向的膜蛋白以及分泌蛋白都使用相同的内质网易位位点，并且Sec61p是这些位点的核心成分。
We have identified membrane components which are adjacent to type I and type II signal-anchor proteins during their insertion into the membrane of the ER. Using two different cross-linking approaches a 37-38-kD nonglycosylated protein, previously identified as P37 (High, S., D. Gorlich, M. Wiedmann, T. A. Rapoport, and B. Dobberstein. 1991. J. Cell Biol. 113:35-44), was found adjacent to all the membrane inserted nascent chains used in this study. On the basis of immunoprecipitation, this ER protein was shown to be identical to the recently identified mammalian Sec61 protein. Thus, Sec61p is the principal cross-linking partner of both type I and type II signal-anchor proteins during their membrane insertion (this work), and of secretory proteins during their translocation (Gorlich, a, S. Prehn, E. Hartmann, K.-U. Kalies, and T. A. Rapoport. 1992. Cell. 71:489-503). We propose that membrane proteins of both orientations, and secretory proteins employ the same ER translocation sites, and that Sec61p is a core component of these sites.