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GTP-dependent ADP-ribosylation of a 22 kDa protein in the endoplasmic reticulum membrane.

作者信息

Robinson A, Austen B

出版信息

FEBS Lett. 1987 Jun 22;218(1):63-7. doi: 10.1016/0014-5793(87)81019-0.

DOI:10.1016/0014-5793(87)81019-0
PMID:3297785
Abstract

Treatment of salt-stripped rough microsomal membranes from pancreas or liver with NAD and cholera toxin in the presence of GTP yields an ADP-ribosylated non-ribosomal 22 kDa protein. Membranes containing the modified protein are less active in the co-translational processing of secretory preproteins translated from isolated mRNA in a reticulocyte translation system, but signal peptidase activity is unchanged, suggesting that the 22 kDa protein is involved in the targetting or translocation of secretory proteins at the membrane of the endoplasmic reticulum.

摘要

相似文献

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引用本文的文献

1
The role of topogenic sequences in the movement of proteins through membranes.拓扑序列在蛋白质跨膜转运中的作用。
Biochem J. 1987 Sep 1;246(2):249-61. doi: 10.1042/bj2460249.
2
Detection of GTP-binding proteins in purified derivatives of rough endoplasmic reticulum.粗面内质网纯化衍生物中GTP结合蛋白的检测
Biochem J. 1989 Sep 1;262(2):497-503. doi: 10.1042/bj2620497.