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GTP‐dependent ADP‐ribosylation of a 22 kDa protein in the endoplasmic reticulum membrane
Author(s) -
Robinson Andrew,
Austen Brian
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81019-0
Subject(s) - endoplasmic reticulum , cholera toxin , biochemistry , reticulocyte , stim1 , adp ribosylation , gtp' , microsome , ribosome , membrane protein , secretory protein , chemistry , biology , microbiology and biotechnology , membrane , nad+ kinase , messenger rna , enzyme , rna , gene
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.